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Статті в журналах з теми "Desmocollins"

Автор: Grafiati

Опубліковано: 3 червня 2025

Оновлено: 31 липня 2025

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1

Muhammad, Javed Khan* Imran Khan Irshad Ali Sheikh Ahmed Ghulam Mustafa Khan. "A REVIEW ON DESMOGLEINS, DESMOCOLLINS AND ASSOCIATED DISEASES." Indo American Journal of Pharmaceutical Sciences 04, no. 11 (2017): 4053–61. https://doi.org/10.5281/zenodo.1045425.

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Анотація:

In most epithelia, desmosomes are important adhesion structures which have a key role in linking the intermediate filament network of one cell to its neighbor, thus forming a strong bond. These junctions are essential for retaining the integrity of organs, subject to mechanical stress, particularly the heart and skin. Desmogleins and desmocollins belong to super family of cadherin, which mediate adhesion at desmosomes. Through a series of protein interactions, desmosomal cadherin tails get associated with Cytoplasmic components of the desmosome, the sites of desmosome assemblage are employed w

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2

Marcozzi, C., I. D. Burdett, R. S. Buxton, and A. I. Magee. "Coexpression of both types of desmosomal cadherin and plakoglobin confers strong intercellular adhesion." Journal of Cell Science 111, no. 4 (1998): 495–509. http://dx.doi.org/10.1242/jcs.111.4.495.

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Desmosomes are unique intercellular junctions in that they invariably contain two types of transmembrane cadherin molecule, desmocollins and desmogleins. In addition they possess a distinct cytoplasmic plaque structure containing a few major proteins including desmoplakins and the armadillo family member plakoglobin. Desmosomal cadherins are putative cell-cell adhesion molecules and we have tested their adhesive capacity using a transfection approach in mouse L cells. We find that L cells expressing either one or both of the desmosomal cadherins desmocollin 2a or desmoglein 1 display weak cell

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3

Wahl, James K. "Desmogleins and Desmocollins as Adhesive Molecules." Journal of Investigative Dermatology 127 (January 2007): E10. http://dx.doi.org/10.1038/sj.skinbio.6250003.

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4

Legan, P. K., K. K. Yue, M. A. Chidgey, J. L. Holton, R. W. Wilkinson, and D. R. Garrod. "The bovine desmocollin family: a new gene and expression patterns reflecting epithelial cell proliferation and differentiation." Journal of Cell Biology 126, no. 2 (1994): 507–18. http://dx.doi.org/10.1083/jcb.126.2.507.

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We have discovered a third bovine desmocollin gene, DSC3, and studied expression of all three desmocollin genes, DSC1, 2, and 3, by Northern blotting, RT-PCR and in situ hybridization. DSC1 is strongly expressed in epidermis and tongue papillae, showing a "skin"-type pattern resembling that previously described for keratins 1 and 10. Expression is absent from the epidermal basal layer but appears in the immediate suprabasal layers and continues uniformly to the lower granular layer. In tongue epithelium, expression is suprabasal and strictly localized to papillae, being absent from interpapill

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5

Arnemann, J., K. H. Sullivan, A. I. Magee, I. A. King, and R. S. Buxton. "Stratification-related expression of isoforms of the desmosomal cadherins in human epidermis." Journal of Cell Science 104, no. 3 (1993): 741–50. http://dx.doi.org/10.1242/jcs.104.3.741.

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Анотація:

Desmosomal junctions are abundant in epidermis and contain two classes of transmembrane glycoprotein, the desmocollins and the desmogleins, which are members of the cadherin superfamily of Ca(2+)-dependent cell adhesion molecules. The desmocollin subfamily includes DGIV/V and DGII/III while the desmoglein subfamily includes DGI, HDGC and the autoantigen of the blistering skin disease pemphigus vulgaris (PVA). There are also several non-glycosylated proteins, including the desmoplakins and plakoglobin, present in the desmosomal plaque, which forms a link between the glycoproteins and the cytoke

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6

North, A. J., W. G. Bardsley, J. Hyam, et al. "Molecular map of the desmosomal plaque." Journal of Cell Science 112, no. 23 (1999): 4325–36. http://dx.doi.org/10.1242/jcs.112.23.4325.

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Анотація:

Recent biochemical and molecular approaches have begun to establish the protein interactions that lead to desmosome assembly. To determine whether these associations occur in native desmosomes we have performed ultrastructural localisation of specific domains of the major desmosomal components and have used the results to construct a molecular map of the desmosomal plaque. Antibodies directed against the amino- and carboxy-terminal domains of desmoplakin, plakoglobin and plakophilin 1, and against the carboxy-terminal domains of desmoglein 3, desmocollin 2a and desmocollin 2b, were used for im

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7

MÃ¼ller, R., B. Heber, T. Hashimoto, et al. "Autoantibodies against desmocollins in European patients with pemphigus." Clinical and Experimental Dermatology 34, no. 8 (2009): 898–903. http://dx.doi.org/10.1111/j.1365-2230.2009.03241.x.

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8

Yue, K. K., J. L. Holton, J. P. Clarke, et al. "Characterisation of a desmocollin isoform (bovine DSC3) exclusively expressed in lower layers of stratified epithelia." Journal of Cell Science 108, no. 6 (1995): 2163–73. http://dx.doi.org/10.1242/jcs.108.6.2163.

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Анотація:

Desmocollins are cadherin-like glycoproteins involved in cell adhesion and plaque formation in desmosome junctions. Three distinct isoforms, the products of different genes, have been found in bovine tissues. We have reported previously that one of these, DSC3, is expressed only in basal and lower suprabasal layers of stratified epithelia. Using RT-PCR we have now obtained the complete cDNA coding sequence of mature bovine DSC3. It has alternatively spliced ‘a’ and ‘b’ forms found in other desmocollins but is unique in having a 43 instead of a 46 base pair exon. We have characterised a monoclo

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9

Harrison, Oliver J., Julia Brasch, Gorka Lasso, et al. "Structural basis of adhesive binding by desmocollins and desmogleins." Proceedings of the National Academy of Sciences 113, no. 26 (2016): 7160–65. http://dx.doi.org/10.1073/pnas.1606272113.

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Анотація:

Desmosomes are intercellular adhesive junctions that impart strength to vertebrate tissues. Their dense, ordered intercellular attachments are formed by desmogleins (Dsgs) and desmocollins (Dscs), but the nature of trans-cellular interactions between these specialized cadherins is unclear. Here, using solution biophysics and coated-bead aggregation experiments, we demonstrate family-wise heterophilic specificity: All Dsgs form adhesive dimers with all Dscs, with affinities characteristic of each Dsg:Dsc pair. Crystal structures of ectodomains from Dsg2 and Dsg3 and from Dsc1 and Dsc2 show bind

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10

Cui, Tiantian, Yuan Chen, Linlin Yang, et al. "Diagnostic and prognostic impact of desmocollins in human lung cancer." Journal of Clinical Pathology 65, no. 12 (2012): 1100–1106. http://dx.doi.org/10.1136/jclinpath-2011-200630.

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11

Geller, Shamir, Andrea Gat, Avikam Harel, et al. "Childhood Pemphigus Foliaceus with Exclusive Immunoglobulin G Autoantibodies to Desmocollins." Pediatric Dermatology 33, no. 1 (2016): e10-e13. http://dx.doi.org/10.1111/pde.12729.

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12

Tay, Y. E., S. S. J. Lee, and Y. L. Lim. "Pemphigus herpetiformis with autoantibodies to desmocollins 1, 2 and 3." Clinical and Experimental Dermatology 43, no. 3 (2018): 360–62. http://dx.doi.org/10.1111/ced.13355.

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13

Dmochowski, M., T. Hashimoto, T. Ebihara, A. Ide, D. R. Garrod, and T. Nishikawa. "Desmocollins I and II are recognized by certain pemphigus autoantibodies." Journal of Dermatological Science 4, no. 2 (1992): 111. http://dx.doi.org/10.1016/0923-1811(92)90082-m.

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14

Stateshnyy, O. N., E. Yu Zlatnik, E. P. Ulyanova, et al. "PROGNOSTIC SIGNIFICANCE OF DESMOCOLLINS` EXPRESSION IN LUNG CARCINOMA OF INOPERABLE PATIENTS." Современные проблемы науки и образования (Modern Problems of Science and Education), no. 2 2023 (2023): 82. http://dx.doi.org/10.17513/spno.32548.

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15

Gallo, E., P. García-Martín, J. Fraga, et al. "Paraneoplastic pemphigus with eosinophilic spongiosis and autoantibodies against desmocollins 2 and 3." Clinical and Experimental Dermatology 39, no. 3 (2014): 323–26. http://dx.doi.org/10.1111/ced.12296.

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16

Suhrbier, A., and D. Garrod. "An investigation of the molecular components of desmosomes in epithelial cells of five vertebrates." Journal of Cell Science 81, no. 1 (1986): 223–42. http://dx.doi.org/10.1242/jcs.81.1.223.

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Анотація:

We have shown previously, by fluorescent antibody staining, that desmosomal antigens are widely distributed in the tissues of vertebrate animals. Furthermore, we have demonstrated mutual desmosome formation between cells derived from man, cow, dog, chicken and frog. In this paper we have studied the components of desmosomes in a tissue or a cell line from each of these animals by immunoblotting with antibodies raised against the desmosomal components isolated from bovine nasal epithelium. Blotting was carried out on bovine nasal epithelial desmosomal cores, desmosome-enriched fractions derived

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17

Mechanic, S., K. Raynor, J. E. Hill, and P. Cowin. "Desmocollins form a distinct subset of the cadherin family of cell adhesion molecules." Proceedings of the National Academy of Sciences 88, no. 10 (1991): 4476–80. http://dx.doi.org/10.1073/pnas.88.10.4476.

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18

Teye, Kwesi, Sanae Numata, Ayaka Ohzono, et al. "Establishment of IgA ELISAs of mammalian recombinant proteins of human desmocollins 1–3." Journal of Dermatological Science 83, no. 1 (2016): 75–77. http://dx.doi.org/10.1016/j.jdermsci.2016.04.001.

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19

Ueda, A., N. Ishii, K. Teye, et al. "Unique herpetiform bullous dermatosis with IgG antibodies to desmocollins 1/3 and LAD-1." British Journal of Dermatology 169, no. 3 (2013): 719–21. http://dx.doi.org/10.1111/bjd.12398.

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20

Bisena Jayashree. "DESMOSOMES IN ORAL DISEASES – A REVIEW." International Journal of Histopathological Interpretation 11, no. 1 (2022): 34–38. http://dx.doi.org/10.56501/intjhistopatholinterpret.v11i1.187.

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Анотація:

Desmosomes are the adhesion proteins that function both as an adhesive complex and as a cell surface attachment site for keratin intermediate filaments of the cytoskeleton. Desmosomes are more widely distributed along the lateral membranes. Desmosomes contain two types of transmembrane proteins desmogleins and desmocollins which belong to cadherin family. These desmosomal cadherins are linked to the keratin cytoskeleton via several cytoplasmic proteins such as desmoplakin and plakoglobin. Desmosomes play a critical role in the maintenance of normal tissue architecture. They are frequently muta

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21

Arai, Rie, Hiroto Okuda, Daisuke Tsuruta, et al. "IgA pemphigus with non-pustular erythematous lesions and IgA antibodies to desmocollins 1 and 2." European Journal of Dermatology 23, no. 3 (2013): 362–65. http://dx.doi.org/10.1684/ejd.2013.2046.

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22

Arnemann, J., N. K. Spurr, and R. S. Buxton. "ATaql RFLP in the N-terminal part of the gene for desmocollins DGII/III (psc)." Nucleic Acids Research 19, no. 22 (1991): 6343. http://dx.doi.org/10.1093/nar/19.22.6343-a.

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23

Hashimoto, Takashi, Masayuki Amagai, Kyoko Watanabe, et al. "A Case of Pemphigus Vulgaris Showing Reactivity with Pemphigus Antigens (Dsg1 and Dsg3) and Desmocollins." Journal of Investigative Dermatology 104, no. 4 (1995): 541–44. http://dx.doi.org/10.1111/1523-1747.ep12606050.

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24

Owen, Gethin R., and David L. Stokes. "Exploring the Nature of Desmosomal Cadherin Associations in 3D." Dermatology Research and Practice 2010 (2010): 1–12. http://dx.doi.org/10.1155/2010/930401.

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Анотація:

Desmosomes are a complex assembly of protein molecules that mediate adhesion between adjacent cells. Desmosome composition is well established and spatial relationships between components have been identified. Intercellular cell-cell adhesion is created by the interaction of extracellular domains of desmosomal cadherins, namely, desmocollins and desmogleins. High-resolution methods have provided insight into the structural interactions between cadherins. However, there is a lack of understanding about the architecture of the intact desmosomes and the physical principles behind their adhesive s

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25

Parrish, E. P., J. E. Marston, D. L. Mattey, H. R. Measures, R. Venning, and D. R. Garrod. "Size heterogeneity, phosphorylation and transmembrane organisation of desmosomal glycoproteins 2 and 3 (desmocollins) in MDCK cells." Journal of Cell Science 96, no. 2 (1990): 239–48. http://dx.doi.org/10.1242/jcs.96.2.239.

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Анотація:

Metabolic labelling with [35S]methionine and immunoprecipitation with specific antibodies to bovine desmosomal glycoproteins 2 and 3 (dg2 and dg3: desmocollins) reveals a triplet of polypeptides of Mr 115,000, 107,000 and 104,000 in MDCK cells. Tunicamycin treatment shows that this heterogeneity does not arise through differential N-linked glycosylation. Under conditions in which cells are actively forming desmosomes, the largest polypeptide, dg2, becomes phosphorylated on serine, but the two smaller polypeptides, dg3a and 3b, do not. Controlled trypsinisation of intact cells yields three memb

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26

Nekrasova, Oxana E., Evangeline V. Amargo, William O. Smith, Jing Chen, Geri E. Kreitzer, and Kathleen J. Green. "Desmosomal cadherins utilize distinct kinesins for assembly into desmosomes." Journal of Cell Biology 195, no. 7 (2011): 1185–203. http://dx.doi.org/10.1083/jcb.201106057.

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Анотація:

The desmosomal cadherins, desmogleins (Dsgs) and desmocollins (Dscs), comprise the adhesive core of intercellular junctions known as desmosomes. Although these adhesion molecules are known to be critical for tissue integrity, mechanisms that coordinate their trafficking into intercellular junctions to regulate their proper ratio and distribution are unknown. We demonstrate that Dsg2 and Dsc2 both exhibit microtubule-dependent transport in epithelial cells but use distinct motors to traffic to the plasma membrane. Functional interference with kinesin-1 blocked Dsg2 transport, resulting in the a

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27

Holton, J. L., T. P. Kenny, P. K. Legan, et al. "Desmosomal glycoproteins 2 and 3 (desmocollins) show N-terminal similarity to calcium-dependent cell-cell adhesion molecules." Journal of Cell Science 97, no. 2 (1990): 239–46. http://dx.doi.org/10.1242/jcs.97.2.239.

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The N-terminal sequence of a mixture of desmosomal glycoproteins 2 and 3 (dg2/3, desmocollins) from bovine nasal epidermis, prepared by electro-elution from polyacrylamide gels, was determined by solid-phase Edman degradation. A sequence of 23 amino acids was obtained. This showed 43% identity with that of the N terminus of the calcium-dependent cell adhesion molecule, N-cadherin. A lesser degree of identity with other members of the cadherin-uvomorulin-L-CAM family was also found. In order to confirm that the sequence was derived from the dg2/3 molecules a rabbit antiserum was raised against

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28

Chen, Jing, Oxana E. Nekrasova, Dipal M. Patel, et al. "The C-terminal unique region of desmoglein 2 inhibits its internalization via tail–tail interactions." Journal of Cell Biology 199, no. 4 (2012): 699–711. http://dx.doi.org/10.1083/jcb.201202105.

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Анотація:

Desmosomal cadherins, desmogleins (Dsgs) and desmocollins, make up the adhesive core of intercellular junctions called desmosomes. A critical determinant of epithelial adhesive strength is the level and organization of desmosomal cadherins on the cell surface. The Dsg subclass of desmosomal cadherins contains a C-terminal unique region (Dsg unique region [DUR]) with unknown function. In this paper, we show that the DUR of Dsg2 stabilized Dsg2 at the cell surface by inhibiting its internalization and promoted strong intercellular adhesion. DUR also facilitated Dsg tail–tail interactions. Forced

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29

Ohata, C., H. Koga, K. Teye, et al. "Concurrence of bullous pemphigoid and herpetiform pemphigus with IgG antibodies to desmogleins 1/3 and desmocollins 1-3." British Journal of Dermatology 168, no. 4 (2012): 879–81. http://dx.doi.org/10.1111/bjd.12019.

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30

Chidgey, Martyn A. J., Jonathan P. Clarke, and David R. Garrod. "Expression of Full-Length Desmosomal Glycoproteins (Desmocollins) Is Not Sufficient to Confer Strong Adhesion on Transfected L929 Cells." Journal of Investigative Dermatology 106, no. 4 (1996): 689–95. http://dx.doi.org/10.1111/1523-1747.ep12345525.

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31

Chorzelski, Tadeusz P., Takashi Hashimoto, Takeji Nishikawa, et al. "Unusual acantholytic bullous dermatosis associated with neoplasia and IgG and IgA antibodies against bovine desmocollins I and II." Journal of the American Academy of Dermatology 31, no. 2 (1994): 351–55. http://dx.doi.org/10.1016/s0190-9622(94)70171-7.

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32

SMITH, Conrad, Kuichun ZHU, Anita MERRITT, et al. "Regulation of desmocollin gene expression in the epidermis: CCAAT/enhancer-binding proteins modulate early and late events in keratinocyte differentiation." Biochemical Journal 380, no. 3 (2004): 757–65. http://dx.doi.org/10.1042/bj20040077.

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Desmocollins (Dscs) are desmosomal cadherins that exhibit differentiation-specific patterns of expression in the epidermis. Dsc3 expression is strongest in basal cell layers, whereas Dsc1 is largely confined to upper, terminally differentiating strata. To understand better the processes by which Dsc expression is regulated in the epidermis, we have isolated Dsc3 and Dsc1 5´-flanking DNAs and analysed their activity in primary keratinocytes. In the present study, we found that transcription factors of the CCAAT/enhancer-binding protein family play a role in the regulation of expression of both

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33

Asahina, A., H. Koga, Y. Suzuki, and T. Hashimoto. "IgA pemphigus associated with diffuse large B-cell lymphoma showing unique reactivity with desmocollins: unusual clinical and histopathological features." British Journal of Dermatology 168, no. 1 (2012): 224–26. http://dx.doi.org/10.1111/j.1365-2133.2012.11127.x.

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34

HASHIMOTO, K., T. HASHIMOTO, M. HIGASHIYAMA, T. NISHIKAWA, D. GARROD, and K. YOSHIKAWA. "Detection of anti-desmocollins I and II autoantibodies in two cases of Hallopeau type pemphigus vegetans by immunoblot analysis." Journal of Dermatological Science 7, no. 2 (1994): 100–106. http://dx.doi.org/10.1016/0923-1811(94)90083-3.

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35

Collins, J. E., P. K. Legan, T. P. Kenny, J. MacGarvie, J. L. Holton, and D. R. Garrod. "Cloning and sequence analysis of desmosomal glycoproteins 2 and 3 (desmocollins): cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains." Journal of Cell Biology 113, no. 2 (1991): 381–91. http://dx.doi.org/10.1083/jcb.113.2.381.

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Анотація:

Desmosomal glycoproteins 2 and 3 (dg2 and 3) or desmocollins have been implicated in desmosome adhesion. We have obtained a 5.0-kb-long clone for dg3 from a bovine nasal epidermal lambda gt11 cDNA library. Sequence analysis of this clone reveals an open reading frame of 2,517 bases encoding a polypeptide of 839 amino acids. The sequence consists of a signal peptide of 28 amino acids, a precursor sequence of 104 amino acids, and a mature protein of 707 amino acids. The latter has the characteristics of a transmembrane glycoprotein with an extracellular domain of 550 amino acids and a cytoplasmi

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36

Dmochowski, Marian, Takashi Hashimoto, David R. Garrod, and Takeji Nishikawa. "Desmocollins I and II Are Recognized by Certain Sera from Patients with Various Types of Pemphigus, Particularly Brazilian Pemphigues Foliaceus." Journal of Investigative Dermatology 100, no. 4 (1993): 380–84. http://dx.doi.org/10.1111/1523-1747.ep12471934.

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37

Teye, Kwesi, Norito Ishii, Hiroshi Koga, et al. "Newly developed IgA ELISAs of eukaryotic recombinant proteins of desmocollins 1-3 are more sensitive and specific than baculoprotein ELISAs." Journal of Dermatological Science 69, no. 2 (2013): e8-e9. http://dx.doi.org/10.1016/j.jdermsci.2012.11.322.

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38

Hashimoto, Takashi, Masayuki Amagai, David R. Garrod, and Takeji Nishikawa. "061 Both IgG and IgA antibodies in sera of various types of pemphigus recognize conformationally sensitive epitopes of human desmocollins." Journal of Dermatological Science 12, no. 2 (1996): 192. http://dx.doi.org/10.1016/0923-1811(96)89464-3.

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39

ADAMS, J. Michael, B. Martin REICHEL, A. Ian KING, et al. "Characterization of the regulatory regions in the human desmoglein genes encoding the pemphigus foliaceous and pemphigus vulgaris antigens." Biochemical Journal 329, no. 1 (1998): 165–74. http://dx.doi.org/10.1042/bj3290165.

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Анотація:

The adhesive proteins in the desmosome type of cell junction consist of two members of the cadherin superfamily, the desmogleins and desmocollins. Both desmogleins and desmocollins occur as at least three different isoforms with various patterns of expression. The molecular mechanisms controlling the differential expression of the desmosomal cadherin isoforms are not yet known. We have begun an investigation of desmoglein gene expression by cloning and analysing the promoters of the human genes coding for the type 1 and type 3 desmogleins (DSG1 and DSG3). The type 1 isoform is restricted to th

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40

King, Ian A., Kate H. Sullivan, Richard Bennett, and Roger S. Buxton. "The Desmocollins of Human Foreskin Epidermis: Identification and Chromosomal Assignment of a Third Gene and Expression Patterns of the Three Isoforms." Journal of Investigative Dermatology 105, no. 3 (1995): 314–21. http://dx.doi.org/10.1111/1523-1747.ep12319935.

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41

Jones, J. C. "Characterization of a 125K glycoprotein associated with bovine epithelial desmosomes." Journal of Cell Science 89, no. 2 (1988): 207–16. http://dx.doi.org/10.1242/jcs.89.2.207.

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An analysis of the concanavalinA binding polypeptide components of bovine tongue epithelial desmosomes reveals that in addition to the known desmosomal glycoproteins of 100/115K (the ‘desmocollins’), 140K and 160/165K (‘desmoglein 1’) there is an uncharacterized glycoprotein of 125K (K = Mr × 10(−3). This latter polypeptide is immunologically distinct from known desmosomal glycoproteins, as determined by Western immunoblotting, but is recognized by an antibody preparation directed against the epithelial cell adhesion molecule E-cadherin. Moreover, the cadherin antibodies recognize a polypeptid

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Yu, Qian-Chun, Elizabeth Allen, and Elaine Fuchs. "Desmosomal Disorganization and Epidermal Abnormalities in a Transgenic Mouse Expressing Mutant Desmoglein-3." Proceedings, annual meeting, Electron Microscopy Society of America 54 (August 11, 1996): 34–35. http://dx.doi.org/10.1017/s0424820100162636.

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Desmosomes are special adhesion structures connecting epithelial cells. The formation of desmosome plaques requires the participation of multiple molecules including desmoplakin (DP), plakoglobin (PG), desmocollins (DSC), and desmogleins (Dsg). It is known that Dsg has functional domains involved in cell-cell adhesions and plaque-cytoskeleton interactions. Functional modulation of Dsg is known to be related to some skin disorders exhibiting desmosome abnormalities. To better understand the role of Dsg 3 in the assembly of epidermal desmosomes and its possible relation to cutaneous disorders, w

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43

Iwasa, Makoto, Koji Hashimoto, Mari Higashiyama, Takashi Hashimoto, and Kunihiko Yoshikawa. "A report of two cases of hallopeau type pemphigus vegetans with detection of anti-desmocollins I and II autoantibodies by immunoblot analysis." Journal of Dermatological Science 6, no. 1 (1993): 106. http://dx.doi.org/10.1016/0923-1811(93)91330-w.

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44

Odani, Kentaro, Akane Itoh, Soshi Yanagita, et al. "Paraneoplastic Pemphigus Involving the Respiratory and Gastrointestinal Mucosae." Case Reports in Pathology 2020 (June 29, 2020): 1–8. http://dx.doi.org/10.1155/2020/7350759.

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Paraneoplastic pemphigus (PNP), an autoimmune mucocutaneous disorder involving the oral and bronchial mucosae, is a rare complication of hematologic malignancy. Serologically, serum autoantibodies against varied desmosome-related proteins are of notice. PNP is often lethal due to bronchiolitis obliterans and opportunistic infection. A 70-year-old Japanese male complained of dry cough, stomatitis, and sore throat. The lips and oral mucosa were severely eroded, and skin eruptions were seen on the chest and abdomen. The biopsy features were consistent with PNP, and the deposition of IgG and IgM w

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SYED, Shabih-e.-Hassnain, Brian TRINNAMAN, Stephen MARTIN, Sarah MAJOR, Jon HUTCHINSON, and Anthony I. MAGEE. "Molecular interactions between desmosomal cadherins." Biochemical Journal 362, no. 2 (2002): 317–27. http://dx.doi.org/10.1042/bj3620317.

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Desmocollins (Dscs) and desmogleins (Dsgs) are cell-adhesion molecules involved in the formation of desmosome cell—cell junctions and share structural similarities to classical cadherins such as E-cadherin. In order to identify and provide quantitative information on the types of protein—protein interactions displayed by the type 2 isoforms and investigate the role of Ca2+ in this process, we have developed an Escherichia coli expression system to generate recombinant proteins containing the first two extracellular domains, namely Dsg2(1-2) and Dsc2(1-2). Analytical ultracentrifugation, chemic

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Kim, Jaehwan, Kwesi Teye, Hiroshi Koga, et al. "Successful single-cycle rituximab treatment in a patient with pemphigus vulgaris and squamous cell carcinoma of the tongue and IgG antibodies to desmocollins." Journal of the American Academy of Dermatology 69, no. 1 (2013): e26-e27. http://dx.doi.org/10.1016/j.jaad.2012.12.967.

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47

Wahl, J. K., J. E. Nieset, P. A. Sacco-Bubulya, T. M. Sadler, K. R. Johnson, and M. J. Wheelock. "The amino- and carboxyl-terminal tails of (beta)-catenin reduce its affinity for desmoglein 2." Journal of Cell Science 113, no. 10 (2000): 1737–45. http://dx.doi.org/10.1242/jcs.113.10.1737.

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beta-catenin and plakoglobin are members of the armadillo family of proteins and were first identified as components of intercellular adhering junctions. In the adherens junction beta-catenin and plakoglobin serve to link classical cadherins to the actin-based cytoskeleton. In the desmosome plakoglobin links the desmosomal cadherins, the desmogleins and the desmocollins, to the intermediate filament cytoskeleton. beta-catenin is not a component of the desmosome. Previously we have shown that the central armadillo repeat region of plakoglobin is the site for desmosomal cadherin binding. We hypo

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48

Garrod, D. R., and S. Fleming. "Early expression of desmosomal components during kidney tubule morphogenesis in human and murine embryos." Development 108, no. 2 (1990): 313–21. http://dx.doi.org/10.1242/dev.108.2.313.

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Developing kidneys of human and murine fetuses have been stained with monoclonal antibodies to desmosomal proteins 1 and 2 (desmoplakins) (dp 1&2), desmosomal glycoprotein 1 (desmoglein) and a polyclonal antiserum to desmosomal glycoproteins 2 and 3 (desmocollins). All three antibodies stain the mesenchymal condensates that represent the first stage in kidney tubule development, indicating that desmosomal antigens are expressed very early in tubule morphogenesis. Desmosomal antigens are continuously expressed throughout the developing tubule being concentrated at the apical and basal regio

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Mattey, D. L., and D. R. Garrod. "Calcium-induced desmosome formation in cultured kidney epithelial cells." Journal of Cell Science 85, no. 1 (1986): 95–111. http://dx.doi.org/10.1242/jcs.85.1.95.

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Previous work has shown that cultured keratinocytes do not form desmosomes at low [Ca2+] (less than 0.1 mM) but may be induced to do so by raising [Ca2+] to physiological levels (1.8-2 mM). Here, fluorescent antibody staining with specific anti-desmosomal antibodies and electron microscopy have been used to determine whether Ca2+-induced desmosome formation also occurs in simple epithelial cells. Both Madin-Darby canine and bovine kidney cells (MDCK and MDBK) exhibit Ca2+-induced desmosome formation, but there are significant differences between them. MDCK cells resemble keratinocytes in showi

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Mattey, D. L., G. Burdge, and D. R. Garrod. "Development of desmosomal adhesion between MDCK cells following calcium switching." Journal of Cell Science 97, no. 4 (1990): 689–704. http://dx.doi.org/10.1242/jcs.97.4.689.

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The development or maturation of intercellular adhesions following their initiation has received very little attention even though this is an area of significance for a variety of in vivo processes. Using Ca2(+)-induced desmosome formation in MDCK cells as a study system it is shown that, following its initiation, desmosome formation continues for many hours. Following Ca2+ switching the major desmosomal glycoproteins, dg2/3a,b (desmocollins), accumulate progressively at the cell surface. Accumulation is first detectable within 45 min, but continues linearly for approximately 16 h, reaching a

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