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Journal articles on the topic 'Collagen variants'

Author: Grafiati

Published: 22 June 2024

Last updated: 31 July 2025

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1

Richards, Allan J., and Martin P. Snead. "Molecular Basis of Pathogenic Variants in the Fibrillar Collagens." Genes 13, no. 7 (2022): 1199. http://dx.doi.org/10.3390/genes13071199.

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The fibrillar collagen family is comprised of the quantitatively major types I, II and III collagens and the quantitatively minor types V and XI. These form heterotypic collagen fibrils (composed of more than a single collagen type) where the minor collagens have a regulatory role in controlling fibril formation and diameter. The structural pre-requisites for normal collagen biosynthesis and fibrillogenesis result in many places where this process can be disrupted, and consequently a wide variety of phenotypes result when pathogenic changes occur in these fibrillar collagen genes. Another cont

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2

Koch, M., B. Bohrmann, M. Matthison, C. Hagios, B. Trueb, and M. Chiquet. "Large and small splice variants of collagen XII: differential expression and ligand binding." Journal of Cell Biology 130, no. 4 (1995): 1005–14. http://dx.doi.org/10.1083/jcb.130.4.1005.

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Collagen XII has a short collagenous tail and a very large, three-armed NC3 domains consisting primarily of fibronectin type III repeats. Differential splicing within this domain gives rise to a large (320 kD) and a small (220 kD) subunit; the large but not the small can carry glycosaminoglycan. To investigate whether collagen XII variants have distinct expression patterns and functions, we generated antibody and cDNA probes specific for the alternatively spliced domain. We report here that the large variant has a more restricted expression in embryonic tissue than the small. For example, wher

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Nishi, Akari, Hikaru Matsui, Azumi Hirata, et al. "Structure, Stability and Binding Properties of Collagen-Binding Domains from Streptococcus mutans." Chemistry 5, no. 3 (2023): 1911–20. http://dx.doi.org/10.3390/chemistry5030130.

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Collagen-binding proteins (CBP), Cnm and Cbm, from Streptococcus mutans are involved in infective endocarditis caused by S. mutans because of their collagen-binding ability. In this study, we focused on the collagen-binding domain (CBD), which is responsible for the collagen-binding ability of CBP, and analyzed its structure, binding activity, and stability using CBD domain variants. The CBD consists of the N1 domain, linker, N2 domain, and latch (N1-N2~) as predicted from the amino acid sequences. The crystal structure of the Cnm/CBD was determined at a 1.81 Å resolution. N1_linker_N2 forms a

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Flood, Veronica H., Abraham C. Schlauderaff, Paula M. Jacobi, et al. "VWF Interaction With Type IV Collagen Is Mediated Through Critical VWF A1 Domain Residues." Blood 122, no. 21 (2013): 29. http://dx.doi.org/10.1182/blood.v122.21.29.29.

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Abstract Von Willebrand factor (VWF) plays a key role in coagulation by tethering platelets to injured subendothelium via binding sites for platelet glycoprotein Ib and collagen. The binding sites for types I and III collagen in the VWF A3 domain are well characterized, and defects in this region have been implicated in von Willebrand disease (VWD). Additional collagens present in the vasculature may also be involved in interactions with VWF. A VWF A1 sequence variation, p.R1399H, has been associated with decreased binding to type VI collagen, but the clinical significance of this observation

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Mikhail, Kristen A., Elizabeth VanSickle, and Linda Z. Rossetti. "Milder presentation of osteogenesis imperfecta type VIII due to compound heterozygosity for a predicted loss-of-function variant and novel missense variant inP3H1—further expansion of the phenotypic spectrum." Molecular Case Studies 9, no. 1 (2023): a006260. http://dx.doi.org/10.1101/mcs.a006260.

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Osteogenesis imperfecta (OI) is a heritable disorder of bone metabolism characterized by multiple fractures with minimal trauma. Autosomal recessive OI type VIII is associated with biallelic pathogenic variants inP3H1and classically characterized by skeletal anomalies in addition to significant bone fragility, sometimes presenting with in utero fractures and/or neonatal lethality.P3H1encodes a collagen prolyl hydroxylase that critically 3-hydroxylates proline residue 986 on the α chain of collagen types I and II to achieve proper folding and assembly of mature collagen and is present in a comp

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Micale, Lucia, Silvia Morlino, Annalisa Schirizzi, et al. "Exon-Trapping Assay Improves Clinical Interpretation of COL11A1 and COL11A2 Intronic Variants in Stickler Syndrome Type 2 and Otospondylomegaepiphyseal Dysplasia." Genes 11, no. 12 (2020): 1513. http://dx.doi.org/10.3390/genes11121513.

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Stickler syndrome (SS) is a hereditary connective tissue disorder affecting bones, eyes, and hearing. Type 2 SS and the SS variant otospondylomegaepiphyseal dysplasia (OSMED) are caused by deleterious variants in COL11A1 and COL11A2, respectively. In both genes, available database information indicates a high rate of potentially deleterious intronic variants, but published evidence of their biological effect is usually insufficient for a definite clinical interpretation. We report four previously unpublished intronic variants in COL11A1 (c.2241 + 5G>T, c.2809 − 2A>G, c.3168 + 5G>C) an

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Shida, Yasuaki, Christine Brown, Jeff Mewburn, et al. "Comprehensive In Vitro and In Vivo Characterization of Loss and Gain-of-Function Von Willebrand Factor Collagen Binding Variants Using a Mouse Model System,." Blood 118, no. 21 (2011): 3266. http://dx.doi.org/10.1182/blood.v118.21.3266.3266.

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Abstract Abstract 3266 Von Willebrand Factor (VWF) is a large multimeric glycoprotein that mediates platelet adhesion to the damaged blood vessel wall and subsequent platelet aggregation at the site of injury. Rare mutations in the VWF A3 domain, that disrupt collagen binding, have been found in patients with a mild bleeding phenotype. However, the analysis of these aberrant VWF-collagen interactions has been relatively limited. Thus, in this study, we have developed mouse models of collagen binding mutants and analyzed the function of the A3 and A1 domains using comprehensive in vitro and in

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López-Márquez, Arístides, Matías Morín, Sergio Fernández-Peñalver, et al. "CRISPR/Cas9-Mediated Allele-Specific Disruption of a Dominant COL6A1 Pathogenic Variant Improves Collagen VI Network in Patient Fibroblasts." International Journal of Molecular Sciences 23, no. 8 (2022): 4410. http://dx.doi.org/10.3390/ijms23084410.

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Collagen VI-related disorders are the second most common congenital muscular dystrophies for which no treatments are presently available. They are mostly caused by dominant-negative pathogenic variants in the genes encoding α chains of collagen VI, a heteromeric network forming collagen; for example, the c.877G>A; p.Gly293Arg COL6A1 variant, which alters the proper association of the tetramers to form microfibrils. We tested the potential of CRISPR/Cas9-based genome editing to silence or correct (using a donor template) a mutant allele in the dermal fibroblasts of four individuals bearing t

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Zhytnik, Lidiia, Binh Ho Duy, Marelise Eekhoff, et al. "Phenotypic Variation in Vietnamese Osteogenesis Imperfecta Patients Sharing a Recessive P3H1 Pathogenic Variant." Genes 13, no. 3 (2022): 407. http://dx.doi.org/10.3390/genes13030407.

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Osteogenesis imperfecta (OI) is a syndromic disorder of bone fragility with high variation in its clinical presentation. Equally variable is molecular aetiology; recessive forms are caused by approximately 20 different genes, many of which are directly implicated in collagen type I biosynthesis. Biallelic variants in prolyl 3-hydroxylase 1 (P3H1) are known to cause severe OI by affecting the competence of the prolyl 3-hydroxylation—cartilage associated protein—peptidyl-prolyl cis-trans isomerase B (P3H1-CRTAP-CyPB) complex, which acts on the Pro986 residue of collagen type I α 1 (COL1A1) and P

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Jäälinoja, Juha, Joni Ylöstalo, William Beckett, David J. S. Hulmes та Leena Ala-Kokko. "Trimerization of collagen IX α-chains does not require the presence of the COL1 and NC1 domains". Biochemical Journal 409, № 2 (2007): 545–54. http://dx.doi.org/10.1042/bj20070984.

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Collagen IX is a heterotrimer of three α-chains, which consists of three COL domains (collagenous domains) (COL1–COL3) and four NC domains (non-collagenous domains) (NC1–NC4), numbered from the C-terminus. Although collagen IX chains have been shown to associate via their C-terminal NC1 domains and form a triple helix starting from the COL1 domain, it is not known whether chain association can occur at other sites and whether other collagenous and non-collagenous regions are involved. To address this question, we prepared five constructs, two long variants (beginning at the NC4 domain) and thr

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Nixon, Thomas R. W., Allan J. Richards, Howard Martin, Philip Alexander, and Martin P. Snead. "Autosomal Recessive Stickler Syndrome." Genes 13, no. 7 (2022): 1135. http://dx.doi.org/10.3390/genes13071135.

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Stickler syndrome (SS) is a genetic disorder with manifestations in the eye, ear, joints, face and palate. Usually inherited in a dominant fashion due to heterozygous pathogenic variants in the collagen genes COL2A1 and COL11A1, it can rarely be inherited in a recessive fashion from variants in COL9A1, COL9A2, and COL9A3, COL11A1, as well as the non-collagen genes LRP2, LOXL3 and GZF1. We review the published cases of recessive SS, which comprise 40 patients from 23 families. Both homozygous and compound heterozygous pathogenic variants are found. High myopia is near-universal, and sensorineur

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Ho, Duy Binh, Lidiia Zhytnik, Katre Maasalu, et al. "Mutation analysis of the COL1A1 and COL1A2 genes in Vietnamese patients with osteogenesis imperfecta." Human Genomics 10, no. 1 (2016): 27. https://doi.org/10.1186/s40246-016-0083-1.

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<strong>Background: </strong>The genetics of osteogenesis imperfecta (OI) have not been studied in a Vietnamese population before. We performed mutational analysis of the <i>COL1A1</i> and <i>COL1A2</i> genes in 91 unrelated OI patients of Vietnamese origin. We then systematically characterized the mutation profiles of these two genes which are most commonly related to OI.<strong>Methods: </strong>Genomic DNA was extracted from EDTA-preserved blood according to standard high-salt extraction methods. Sequence analysis and pathogenic variant identification was performed with Mutation Surveyor DN

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Hayashi, Kaichi, Takeaki Ikeuchi, Ryo Morishita, et al. "The roles of histidine and tyrosine residues in the active site of collagenase in Grimontia hollisae." Journal of Biochemistry 168, no. 4 (2020): 385–92. http://dx.doi.org/10.1093/jb/mvaa055.

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Abstract Collagenase from the Grimontia hollisae strain 1706B (Ghcol) is a zinc metalloproteinase with the zinc-binding motif H492EXXH496. It exhibits higher collagen-degrading activity than the collagenase from Clostridium histolyticum, which is widely used in industry. We previously examined the pH and temperature dependencies of Ghcol activity; Glu493 was thought to contribute acidic pKa (pKe1), while no residue was assigned to contribute alkaline pKa (pKe2). In this study, we introduced nine single mutations at the His or Tyr residues in and near the active site. Our results showed that H4

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14

Castroflorio, Enrico, Ana Joaquina Pérez Berná, Arístides López-Márquez, et al. "The Capillary Morphogenesis Gene 2 Triggers the Intracellular Hallmarks of Collagen VI-Related Muscular Dystrophy." International Journal of Molecular Sciences 23, no. 14 (2022): 7651. http://dx.doi.org/10.3390/ijms23147651.

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Collagen VI-related disorders (COL6-RD) represent a severe form of congenital disease for which there is no treatment. Dominant-negative pathogenic variants in the genes encoding α chains of collagen VI are the main cause of COL6-RD. Here we report that patient-derived fibroblasts carrying a common single nucleotide variant mutation are unable to build the extracellular collagen VI network. This correlates with the intracellular accumulation of endosomes and lysosomes triggered by the increased phosphorylation of the collagen VI receptor CMG2. Notably, using a CRISPR-Cas9 gene-editing tool to

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L. Agustina, A. Miatmoko, R. R. Tjandrawinata, and D. M. Hariyadi. "THE INFLUENCE OF COLLAGEN PEPTIDE VARIANTS ON COLLAGEN PEPTIDE-LOADED ALGINATE MICROSPHERE CHARACTERISTICS." RASAYAN Journal of Chemistry 18, no. 01 (2025): 86–92. https://doi.org/10.31788/rjc.2025.1819054.

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Aging is characterized by decreased collagen production. Collagen peptide is a hydrolyzed product of collagen. The topical peptide collagen could act as anti-aging, however, only a small concentration of peptide collagen could penetrate the skin. A microsphere is a micro-spherical particle that could increase the penetration of molecules via a transcellular pathway. This present study aims to optimize the microsphere formation of various collagen peptides as active agents, using alginate as a polymer and CaCl2 as a cross-linker. The microsphere was prepared with collagen peptide (CP), hydrolyz

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Padmanabha, Hansashree, Gautham Arunachal, Pratik Kishore, et al. "Collagen XII-Related Myopathy: An Emerging Spectrum of Extracellular Matrix-Related Myopathy." Neurology India 71, no. 6 (2023): 1257–59. http://dx.doi.org/10.4103/0028-3886.391402.

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Collagen XII, a member of a protein family called fibril associated collagen with interrupted triple helices (FACIT), is an important component of extracellular matrix and is essential for bridging the neighbouring fibrils. Mutations in collagen XII have been recently described to cause a rare extracellular matrix-related myopathy in those whose phenotype resembles collagen VI-related dystrophies and were negative for pathogenic variants in COL6A genes. The authors report a 4-year old girl presented with a phenotype mimicking Ullrich congenital muscular dystrophy and genetically confirmed to h

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17

Bauer, Anina, John F. Bateman, Shireen R. Lamandé, et al. "Identification of Two Independent COL5A1 Variants in Dogs with Ehlers–Danlos Syndrome." Genes 10, no. 10 (2019): 731. http://dx.doi.org/10.3390/genes10100731.

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The Ehlers–Danlos syndromes (EDS) are a heterogeneous group of heritable disorders affecting connective tissues. The mutations causing the various forms of EDS in humans are well characterized, but the genetic mutations causing EDS-like clinical pathology in dogs are not known, thus hampering accurate clinical diagnosis. Clinical analysis of two independent cases of skin hyperextensibility and fragility, one with pronounced joint hypermobility was suggestive of EDS. Whole-genome sequencing revealed de novo mutations of COL5A1 in both cases, confirming the diagnosis of the classical form of EDS

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Tohar, Ran, Tamar Ansbacher, Inbal Sher, Livnat Afriat-Jurnou, Evgeny Weinberg, and Maayan Gal. "Screening Collagenase Activity in Bacterial Lysate for Directed Enzyme Applications." International Journal of Molecular Sciences 22, no. 16 (2021): 8552. http://dx.doi.org/10.3390/ijms22168552.

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Collagenases are essential enzymes capable of digesting triple-helical collagen under physiological conditions. These enzymes play a key role in diverse physiological and pathophysiological processes. Collagenases are used for diverse biotechnological applications, and it is thus of major interest to identify new enzyme variants with improved characteristics such as expression yield, stability, or activity. The engineering of new enzyme variants often relies on either rational protein design or directed enzyme evolution. The latter includes screening of a large randomized or semirational genet

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Haberichter, Sandra L., David A. Jakab, and Paula M. Jacobi. "Upstream Mechanisms Causing Type 1C Von Willebrand Disease (VWD): Contribution Of Defective Von Willebrand Factor (VWF) Multimerization, Regulated Storage, and Secretion." Blood 122, no. 21 (2013): 3571. http://dx.doi.org/10.1182/blood.v122.21.3571.3571.

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Abstract One mechanism causing type 1 VWD is the reduced survival of VWF in plasma (type 1C VWD), characterized by markedly decreased VWF:Ag and VWF half-life, essentially normal multimers, increased ratio of VWF propeptide (VWFpp) to VWF:Ag, robust response to DDAVP, and normal ratios of VWF:CB, FVIII, or VWF:RCo to VWF:Ag. We enrolled 502 index cases with a pre-existing diagnosis of type 1 VWD through the Zimmerman Program for the Molecular and Clinical Biology of VWD. We confirmed 262 of the index cases as type 1 VWD (VWF:Ag or VWF:RCo ≤ 40 IU/dL). Of these, 58 met the criteria for type 1C

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Annis, Douglas S., Pamela R. Westmark, Christina E. Amend, Brianna Torres, and John P. Sheehan. "Interaction between Collagen IV and Heparin-Binding Sites in the Activity, Distribution and Clearance of Factor IX(a)." Blood 144, Supplement 1 (2024): 2574. https://doi.org/10.1182/blood-2024-211131.

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Introduction: Factor IX (FIX) is unique among vitamin K-dependent coagulation factors in that a substantial portion is bound to extravascular sites. The extravascular compartment of the hemophilia B (HemB) mouse can bind ~3-fold more FIX than is present in plasma and contributes to in vivo hemostasis. FIX Gla domain variants with decreased (K5A) or increased (K5R) collagen IV binding were evaluated in combination with the protease domain variant K126A/K132A, which disrupts heparin binding, to assess effects on extravascular binding of FIX(a). Methods: Human FIX wild type (WT), K5A, K5R, K126A/

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Marinella, Gemma, Guja Astrea, Bianca Buchignani, et al. "A Schematic Approach to Defining the Prevalence of COL VI Variants in Five Years of Next-Generation Sequencing." International Journal of Molecular Sciences 23, no. 23 (2022): 14567. http://dx.doi.org/10.3390/ijms232314567.

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Objective: To define the prevalence of variants in collagen VI genes through a next-generation sequencing (NGS) approach in undiagnosed patients with suspected neuromuscular disease and to propose a diagnostic flowchart to assess the real pathogenicity of those variants. Methods: In the past five years, we have collected clinical and molecular information on 512 patients with neuromuscular symptoms referred to our center. To pinpoint variants in COLVI genes and corroborate their real pathogenicity, we sketched a multistep flowchart, taking into consideration the bioinformatic weight of the gen

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Zekavat, Seyedeh Maryam, Elizabeth L. Chou, Melica Zekavat, et al. "Fibrillar Collagen Variants in Spontaneous Coronary Artery Dissection." JAMA Cardiology 7, no. 4 (2022): 396. http://dx.doi.org/10.1001/jamacardio.2022.0001.

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Selvam, Pavalan, Shekhar Singh, Angita Jain, Herjot Atwal, and Paldeep S. Atwal. "Novel COL11A2 Pathogenic Variants in a Child with Autosomal Recessive Otospondylomegaepiphyseal Dysplasia: A Review of the Literature." Journal of Pediatric Genetics 09, no. 02 (2019): 117–20. http://dx.doi.org/10.1055/s-0039-1698446.

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AbstractOtospondylomegaepiphyseal dysplasia (OSMED) is an inherited autosomal dominant and recessive skeletal dysplasia caused by both heterozygous and homozygous pathogenic variants in COL11A2 encoding the α2(XI) collagen chains, a part of type XI collagen. Here, we describe a 2-year-old girl presenting from birth with a phenotype suggestive of OSMED. On whole exome sequence analysis of the family via commercially available methods, we detected two novel heterozygous pathogenic variants in the proband. In addition, we reviewed the phenotype of autosomal recessive OSMED cases with COL11A2 path

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Kiener, Sarah, Heather Troyer, Daniel Ruvolo, et al. "Independent COL17A1 Variants in Cats with Junctional Epidermolysis Bullosa." Genes 14, no. 10 (2023): 1835. http://dx.doi.org/10.3390/genes14101835.

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Epidermolysis bullosa (EB), characterized by defective adhesion of the epidermis to the dermis, is a heterogeneous disease with many subtypes in human patients and domestic animals. We investigated two unrelated cats with recurring erosions and ulcers on ear pinnae, oral mucosa, and paw pads that were suggestive of EB. Histopathology confirmed the diagnosis of EB in both cats. Case 1 was severe and had to be euthanized at 5 months of age. Case 2 had a milder course and was alive at 11 years of age at the time of writing. Whole genome sequencing of both affected cats revealed independent homozy

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Brown, J. C., K. Mann, H. Wiedemann, and R. Timpl. "Structure and binding properties of collagen type XIV isolated from human placenta." Journal of Cell Biology 120, no. 2 (1993): 557–67. http://dx.doi.org/10.1083/jcb.120.2.557.

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Collagen XIV was isolated from neutral salt extracts of human placenta and purified by several chromatographic steps including affinity binding to heparin. The same procedures also led to the purification of a tissue form of fibronectin. Collagen XIV was demonstrated by partial sequence analysis of its Col1 and Col2 domains and by electron microscopy to be a disulphide-linked molecule with a characteristic cross-shape. The individual chains had a size of approximately 210 kD, which was reduced to approximately 180 kD (domain NC3) after treatment with bacterial collagenase. Specific antibodies

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Kiener, Sarah, Neoklis Apostolopoulos, Jennifer Schissler, et al. "Independent COL5A1 Variants in Cats with Ehlers-Danlos Syndrome." Genes 13, no. 5 (2022): 797. http://dx.doi.org/10.3390/genes13050797.

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We investigated four cats with similar clinical skin-related signs strongly suggestive of Ehlers-Danlos syndrome (EDS). Cases no. 1 and 4 were unrelated and the remaining two cases, no. 2 and 3, were reportedly siblings. Histopathological changes were characterized by severely altered dermal collagen fibers. Transmission electron microscopy in one case demonstrated abnormalities in the collagen fibril organization and structure. The genomes of the two unrelated affected cats and one of the affected siblings were sequenced and individually compared to 54 feline control genomes. We searched for

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Bruni, Valentina, Cristina Barbara Spoleti, Andrea La Barbera, et al. "A Novel Splicing Variant of COL2A1 in a Fetus with Achondrogenesis Type II: Interpretation of Pathogenicity of In-Frame Deletions." Genes 12, no. 9 (2021): 1395. http://dx.doi.org/10.3390/genes12091395.

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Achondrogenesis type II (ACG2) is a lethal skeletal dysplasia caused by dominant pathogenic variants in COL2A1. Most of the variants found in patients with ACG2 affect the glycine residue included in the Gly-X-Y tripeptide repeat that characterizes the type II collagen helix. In this study, we reported a case of a novel splicing variant of COL2A1 in a fetus with ACG2. An NGS analysis of fetal DNA revealed a heterozygous variant c.1267-2_1269del located in intron 20/exon 21. The variant occurred de novo since it was not detected in DNA from the blood samples of parents. We generated an appropri

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O'Connell, Kevin, Michael Posthumus, and Malcolm Collins. "Collagen gene interactions and endurance running performance." South African Journal of Sports Medicine 26, no. 1 (2014): 9. http://dx.doi.org/10.17159/2413-3108/2014/v26i1a404.

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Background. Although variants within genes that encode protein components of several biological systems have been associated with athletic performance, limited studies have investigated the collagen genes that encode the structural components of connective tissues.Objective. To investigate the association of variants within collagen genes with endurance performance in South African (SA) Ironman triathletes.Methods. A total of 661 white, male participants were recruited from four SA Ironman triathlon events for this genetic case-control association study. All participants were genotyped for COL

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O'Connell, Kevin, Michael Posthumus, and Malcolm Collins. "Collagen gene interactions and endurance running performance." South African Journal of Sports Medicine 26, no. 1 (2014): 9–14. https://doi.org/10.17159/2078-516x/2014/v26i1a404.

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Background. Although variants within genes that encode protein components of several biological systems have been associated with athletic performance, limited studies have investigated the collagen genes that encode the structural components of connective tissues.Objective. To investigate the association of variants within collagen genes with endurance performance in South African (SA) Ironman triathletes.Methods. A total of 661 white, male participants were recruited from four SA Ironman triathlon events for this genetic case-control association study. All participants were genotyped for COL

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Tonk, Sahil S., and Golder N. Wilson. "Similar Ehlers–Danlos Syndrome Profiles Produced by Variants in Multiple Collagen Genes." DNA 5, no. 1 (2025): 11. https://doi.org/10.3390/dna5010011.

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Background: Despite increased attention to double-jointedness or joint hypermobility as seen in connective tissue dysplasias like Ehlers–Danlos syndrome, improved clinical DNA correlations are needed to reduce decadal delays in diagnosis. Methods: To this end, patterns of history (among 80) and physical (among 40) findings are compared for 121 Ehlers–Danlos syndrome patients with recurring variants in collagen type I, II, III, V, VI, VII, IX, XI, and XII genes and novel ones in type XV, XVII, XVIII, and XXVII. Results: A recognizable tissue laxity–dysautonomia profile that transcended collagen

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Rigato, Matteo, Carlotta Caprara, J. Said Cabrera-Aguilar, et al. "Collagen Type IV Variants and Kidney Cysts: Decoding the COL4A Puzzle." Genes 16, no. 6 (2025): 642. https://doi.org/10.3390/genes16060642.

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Pathogenic variants in type IV collagen genes (COL4A3, COL4A4, COL4A5) are classically associated with Alport syndrome (AS), a hereditary nephropathy primarily affecting the glomerular basement membrane (GBM). Recent findings, however, suggest a broader phenotypic spectrum that includes renal cyst formation, raising questions about overlapping mechanisms with other cystic kidney diseases. Clinically, renal cysts have been increasingly reported in patients with autosomal dominant and X-linked forms of Alport syndrome, particularly in association with glycine missense variants. The most recent s

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Graves, Lara E., Christie-Lee Wall, Julie N. Briody, et al. "High Bone Mineral Density Osteogenesis Imperfecta in a Family with a Novel Pathogenic Variant in COL1A2." Hormone Research in Paediatrics 93, no. 4 (2020): 263–71. http://dx.doi.org/10.1159/000510463.

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Osteogenesis imperfecta (OI) is a heterogenous group of heritable bone dysplasias characterized by bone fragility, typically low bone mass, joint laxity, easy bruising, and variable short stature. Classical OI is caused by autosomal dominant pathogenic variants in <i>COL1A1</i> or <i>COL1A2</i> that result in either reduced production of normal type 1 collagen or structurally abnormal collagen molecules. Pathogenic variants in these genes generally result in low bone mass. Here, we report a family that had 2 affected individuals who presented with minimal trauma fractur

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Shulman, Cole, Emerald Liang, Misato Kamura, et al. "Type IV Collagen Variants in CKD: Performance of Computational Predictions for Identifying Pathogenic Variants." Kidney Medicine 3, no. 2 (2021): 257–66. http://dx.doi.org/10.1016/j.xkme.2020.12.007.

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Tang, Man-Hung Eric, Joseph P. M. Blair, Cecilie Liv Bager, et al. "Matrix metalloproteinase-degraded type I collagen is associated with APOE/TOMM40 variants and preclinical dementia." Neurology Genetics 6, no. 5 (2020): e508. http://dx.doi.org/10.1212/nxg.0000000000000508.

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ObjectiveDysregulation of type I collagen metabolism has a great impact on human health. We have previously seen that matrix metalloproteinase–degraded type I collagen (C1M) is associated with early death and age-related pathologies. To dissect the biological impact of type I collagen dysregulation, we have performed a genome-wide screening of the genetic factors related to type I collagen turnover.MethodsPatient registry data and genotypes have been collected for a total of 4,981 Danish postmenopausal women. Genome-wide association with serum levels of C1M was assessed and phenotype-genotype

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Powell, Janet T., Jane Adamson, Shane T. R. MacSweeney, Roger M. Greenhalgh, Steven E. Humphries, and Adriano Henney. "Genetic variants of collagen III and abdominal aortic aneurysm." European Journal of Vascular Surgery 5, no. 2 (1991): 145–48. http://dx.doi.org/10.1016/s0950-821x(05)80679-6.

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Sykes, B., D. Ogilvie, P. Wordsworth, and R. Smith. "Polymorphic variants of the human type II collagen gene." Bone 7, no. 2 (1986): 150. http://dx.doi.org/10.1016/8756-3282(86)90705-2.

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Dada, Suhail, Marilize C. Burger, Franka Massij, Hanli de Wet, and Malcolm Collins. "Carpal tunnel syndrome: The role of collagen gene variants." Gene 587, no. 1 (2016): 53–58. http://dx.doi.org/10.1016/j.gene.2016.04.030.

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Lanktree, Matthew B., Amirreza Haghighi, Saima Khowaja, Ioan-Andrei Iliuta, Andrew Paterson, and York P. Pei. "Type IV Collagen Variants in Patients With Polycystic Kidneys." Journal of the American Society of Nephrology 33, no. 11S (2022): 152. http://dx.doi.org/10.1681/asn.20223311s1152a.

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Shulman, Cole, Emerald Liang, Misato Kamura, et al. "In Silico Prediction Performance for Type IV Collagen Variants." Journal of the American Society of Nephrology 31, no. 10S (2020): 526–27. http://dx.doi.org/10.1681/asn.20203110s1526d.

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40

Abdulla, Farah, Heather Peck, Ashley Feneran, Ashley Jenkins, and Katherine Mullersman. "Distinguishing a Rare Variant of Lipidized Dermatofibroma from Nonlipidized Dermatofibromas in a Patient with Hypothyroidism and Alopecia Areata." Serbian Journal of Dermatology and Venereology 9, no. 2 (2017): 53–56. http://dx.doi.org/10.1515/sjdv-2017-0008.

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Abstract Introduction. Lipidized dermatofibromas represent rare and often underrecognized variants of dermatofibromas. Histologically, dermatofibromas are composed of fibroblast-like spindle cells, foam cells, giant cells, siderophages, lymphocytes, capillaries, collagen fibers, and hyaline dermal collagen fibers. Lipidized dermatofibromas are characterized by numerous foam cells, Touton giant cells, and hyalinized wiry collagen in the stroma. Case report. We present a case of a 31-year-old woman with a history of hypothyroidism and alopecia areata, presenting with an enlarging 8 mm, firm eryt

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Aksyonova, M. E., N. E. Konkova, O. R. Piruzeyeva, et al. "Genetic variants of X-linked Alport syndrome in children: a single-center cohort study." Pediatria. Journal named after G.N. Speransky 103, no. 4 (2024): 25–30. http://dx.doi.org/10.24110/0031-403x-2024-103-4-25-30.

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X-linked Alport syndrome (XLAS) is a monogenic disease characterized by the progressive nephropathy development, sensorineural hearing loss and the lens and retina pathology. The clinical manifestations of the syndrome and the renal prognosis of patients are determined by the nature of the gene COL4A5 mutation. The range of COL4A5 genetic variants is different among populations. Information about the XLAS genetic structure in Russian pediatric cohort is insufficient. The purpose of this research was to determine the features of the spectrum of the gene COL4A5 genetic variants in children with

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Ritelli, Marco, Valeria Cinquina, Marina Venturini, et al. "Expanding the Clinical and Mutational Spectrum of Recessive AEBP1-Related Classical-Like Ehlers-Danlos Syndrome." Genes 10, no. 2 (2019): 135. http://dx.doi.org/10.3390/genes10020135.

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Ehlers-Danlos syndrome (EDS) comprises clinically heterogeneous connective tissue disorders with diverse molecular etiologies. The 2017 International Classification for EDS recognized 13 distinct subtypes caused by pathogenic variants in 19 genes mainly encoding fibrillar collagens and collagen-modifying or processing proteins. Recently, a new EDS subtype, i.e., classical-like EDS type 2, was defined after the identification, in six patients with clinical findings reminiscent of EDS, of recessive alterations in AEBP1, which encodes the aortic carboxypeptidase–like protein associating with coll

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Sivapalaratnam, Suthesh, Hayman Melissa, Claire Lentaigne, et al. "Congenital Aspirin-like Defect As a Result of Autosomal Recessive Variants in PTGS1." Blood 132, Supplement 1 (2018): 1156. http://dx.doi.org/10.1182/blood-2018-99-118958.

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Abstract Inherited defects of platelet function disorders are rare and difficult to diagnose due to lack of standardized platelet tests. An aspirin-like platelet defect is characterised by reduced thromboxane A2 (TXA2) signalling due to a defect in the arachidonic acid (AA) pathway in platelets. Patients with aspirin-like defect present with mild to moderate bleeding symptoms and impaired platelet aggregation responses to AA and ADP. This is similar to the irreversible effect of aspirin on platelets, which is mediated through inhibition of prostaglandin H synthase-1 also known as cyclooxygenas

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Savige, Judy, Helen Storey, Elizabeth Watson, et al. "Consensus statement on standards and guidelines for the molecular diagnostics of Alport syndrome: refining the ACMG criteria." European Journal of Human Genetics 29, no. 8 (2021): 1186–97. http://dx.doi.org/10.1038/s41431-021-00858-1.

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AbstractThe recent Chandos House meeting of the Alport Variant Collaborative extended the indications for screening for pathogenic variants in the COL4A5, COL4A3 and COL4A4 genes beyond the classical Alport phenotype (haematuria, renal failure; family history of haematuria or renal failure) to include persistent proteinuria, steroid-resistant nephrotic syndrome, focal and segmental glomerulosclerosis (FSGS), familial IgA glomerulonephritis and end-stage kidney failure without an obvious cause. The meeting refined the ACMG criteria for variant assessment for the Alport genes (COL4A3–5). It iden

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Barbeau, Susie, Fannie Semprez, Alexandre Dobbertin, et al. "Molecular Analysis of a Congenital Myasthenic Syndrome Due to a Pathogenic Variant Affecting the C-Terminus of ColQ." International Journal of Molecular Sciences 24, no. 22 (2023): 16217. http://dx.doi.org/10.3390/ijms242216217.

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Congenital Myasthenic Syndromes (CMSs) are rare inherited diseases of the neuromuscular junction characterized by muscle weakness. CMSs with acetylcholinesterase deficiency are due to pathogenic variants in COLQ, a collagen that anchors the enzyme at the synapse. The two COLQ N-terminal domains have been characterized as being biochemical and functional. They are responsible for the structure of the protein in the triple helix and the association of COLQ with acetylcholinesterase. To deepen the analysis of the distal C-terminal peptide properties and understand the CMSs associated to pathogeni

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Chiarelli, Ritelli, Zoppi, and Colombi. "Cellular and Molecular Mechanisms in the Pathogenesis of Classical, Vascular, and Hypermobile Ehlers‒Danlos Syndromes." Genes 10, no. 8 (2019): 609. http://dx.doi.org/10.3390/genes10080609.

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The Ehlers‒Danlos syndromes (EDS) constitute a heterogenous group of connective tissue disorders characterized by joint hypermobility, skin abnormalities, and vascular fragility. The latest nosology recognizes 13 types caused by pathogenic variants in genes encoding collagens and other molecules involved in collagen processing and extracellular matrix (ECM) biology. Classical (cEDS), vascular (vEDS), and hypermobile (hEDS) EDS are the most frequent types. cEDS and vEDS are caused respectively by defects in collagen V and collagen III, whereas the molecular basis of hEDS is unknown. For these d

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Ghasemi, Mohammad-Reza, Maryam Mirahmadi, Hadi Bayat, et al. "Exploring the Genetic Landscape of Knobloch Syndrome: Novel Variant Identification and Literature Review." OBM Genetics 09, no. 02 (2025): 1–36. https://doi.org/10.21926/obm.genet.2502291.

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Knobloch Syndrome (KS) is a rare genetic disorder characterized by ocular abnormalities and central nervous system (CNS) defects, which are attributed to collagenopathy. The primary gene implicated in KS is <em>COL18A1</em>, which encodes the alpha chain of type XVIII collagen. This type of collagen functions as a proteoglycan, predominantly located in the basement membrane of human tissues. This study examined an Iranian female presenting with symptoms of horizontal nystagmus, strabismus, and suspected vision loss, with a potential diagnosis of KS. Genomic DNA was subjected to who

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Villar-Quiles, Rocío N., Sandra Donkervoort, Alix de Becdelièvre, et al. "Clinical and Molecular Spectrum Associated with COL6A3 c.7447A>G p.(Lys2483Glu) Variant: Elucidating its Role in Collagen VI-related Myopathies." Journal of Neuromuscular Diseases 8, no. 4 (2021): 633–45. http://dx.doi.org/10.3233/jnd-200577.

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Background: Dominant and recessive autosomal pathogenic variants in the three major genes (COL6A1-A2-A3) encoding the extracellular matrix protein collagen VI underlie a group of myopathies ranging from early-onset severe conditions (Ullrich congenital muscular dystrophy) to milder forms maintaining independent ambulation (Bethlem myopathy). Diagnosis is based on the combination of clinical presentation, muscle MRI, muscle biopsy, analysis of collagen VI secretion, and COL6A1-A2-A3 genetic analysis, the interpretation of which can be challenging. Objective: To refine the phenotypical spectrum

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Aksenova, M. E., P. E. Povilaitite, N. E. Konkova, and V. V. Dlin. "Diagnostic Value of Type IV Collagen Expression in Renal Glomeruli at Alport’s Syndrome." Rossiyskiy Vestnik Perinatologii i Pediatrii (Russian Bulletin of Perinatology and Pediatrics) 65, no. 6 (2021): 42–49. http://dx.doi.org/10.21508/1027-4065-2020-65-6-42-49.

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The Alport’s syndrome is the hereditary multisystem disease characterized by the development of the progressive nephropathy. The early diagnosis and subsequent prescription of nephroprotective therapy improves significantly the nephrological prognosis. Purpose of the Study. Determine the value of the immunohistochemical method for the Alport’s syndrome diagnosis. Material and methods. The clinical, laboratory and morphological data of 35 patients with suspected Alport’s syndrome (13 years of age [11; 16]; 18 boys and 17 girls) examined in the Nephrology Department in 2013–2019 were summarized.

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Hoyer, M., N. Drechsel, M. Meyer, et al. "Embroidered polymer–collagen hybrid scaffold variants for ligament tissue engineering." Materials Science and Engineering: C 43 (October 2014): 290–99. http://dx.doi.org/10.1016/j.msec.2014.07.010.

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