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Artículos de revistas sobre el tema "Major histocompatibility complex; Antigens"

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Publicado: 4 de junio de 2021

Última modificación: 6 de febrero de 2022

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1

Propper, D. J., M. C. Jones, K. N. Stewart, G. R. D. Catto, and D. A. Power. "Cyclosporin A and the humoral response to blood transfusion in the rat: definition of antigens which suppress alloantibody formation." Clinical Science 80, no. 1 (1991): 9–15. http://dx.doi.org/10.1042/cs0800009.

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1. Blood transfusions improve renal allograft survival rates, but may induce antibodies which are directed to class I major histocompatibility complex antigens and mediate hyperacute transplant rejection. A model to study the development of such antibodies was developed in inbred strains of rats. 2. The influence of transplantation antigens shared between an initial course of blood transfusions, given with cyclosporin A, and a subsequent antigenic challenge (blood transfusion), given without cyclosporin A, on alloantibody responses to class I major histocompatibility complex antigens was then

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2

Ayala García, Marco Antonio, Beatriz González Yebra, Andrea Liliana López Flores, and Eduardo Guaní Guerra. "The Major Histocompatibility Complex in Transplantation." Journal of Transplantation 2012 (2012): 1–7. http://dx.doi.org/10.1155/2012/842141.

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The transplant of organs is one of the greatest therapeutic achievements of the twentieth century. In organ transplantation, the adaptive immunity is considered the main response exerted to the transplanted tissue, since the principal target of the immune response is the MHC (major histocompatibility complex) molecules expressed on the surface of donor cells. However, we should not forget that the innate and adaptive immunities are closely interrelated and should be viewed as complementary and cooperating. When a human transplant is performed, HLA (human leukocyte antigens) molecules from a do

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3

Donaldson, W. L., C. H. Zhang, J. G. Oriol, and D. F. Antczak. "Invasive equine trophoblast expresses conventional class I major histocompatibility complex antigens." Development 110, no. 1 (1990): 63–71. http://dx.doi.org/10.1242/dev.110.1.63.

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Monoclonal antibodies and alloantisera were used in an indirect immunohistochemical assay to determine the expression of class I and class II Major Histocompatibility Complex (MHC) antigens by equine placental cells and the endometrial tissues at the fetal-maternal interface. MHC class I antigens were expressed at high density on the surface of the trophoblast cells of the chorionic girdle at days 32–36, just prior to their invasion of the endometrium. The mature gonadotrophin-secreting cells of the endometrial cups, which are derived from the chorionic girdle cells, had greatly reduced levels

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4

Yang, Young. "Generation of major histocompatibility complex class I antigens." Microbes and Infection 5, no. 1 (2003): 39–47. http://dx.doi.org/10.1016/s1286-4579(02)00050-3.

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5

Steinhoff, Gustav. "Major histocompatibility complex antigens in human liver transplants." Journal of Hepatology 11, no. 1 (1990): 9–15. http://dx.doi.org/10.1016/0168-8278(90)90264-r.

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6

Guillet, Jean-Gerrard, Ming-Zong Lai, Thomas J. Briner, John A. Smith, and Malcolm L. Gefter. "Interaction of peptide antigens and class II major histocompatibility complex antigens." Nature 324, no. 6094 (1986): 260–62. http://dx.doi.org/10.1038/324260a0.

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7

Akbasak, Aytac, Edward H. Oldfield, and Stephen C. Saris. "Expression and modulation of major histocompatibility antigens on murine primary brain tumor in vitro." Journal of Neurosurgery 75, no. 6 (1991): 922–29. http://dx.doi.org/10.3171/jns.1991.75.6.0922.

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✓ Lysis of tumor cells by activated cytotoxic lymphocytes requires their recognition of antigens associated with major histocompatibility complex molecules. The authors studied the constitutive expression of Class I and Class II major histocompatibility complex antigens on mouse brain-tumor cells and the capacity of different cytokines and cytokine combinations to alter this expression in vitro. Cells from the murine glioma 26 (GL26), glioma 261 (GL261), and ependymoblastoma A (EpA) cell lines were established in monolayer culture and treated for 48 hours with either alpha interferon, gamma in

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8

Khoroshkeeva, Khoroshkeeva O. V., Tetruashvili N. K. Tetruashvili, Burmenskaya O. V. Burmenskaya, Agadzhanova A. A. Agadzhanova, and Trofimov D. Yu Trofimov. "Role of major histocompatibility complex antigens in recurrent miscarriage." Akusherstvo i ginekologiia 3_2016 (March 27, 2016): 5–10. http://dx.doi.org/10.18565/aig.2016.3.5-10.

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9

Stroynowski, Iwona. "Molecules Related to Class-I Major Histocompatibility Complex Antigens." Annual Review of Immunology 8, no. 1 (1990): 501–30. http://dx.doi.org/10.1146/annurev.iy.08.040190.002441.

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10

Sinigaglia, F., and J. Hammer. "Predicting major histocompatibility complex-binding sequences within protein antigens." Biochemical Society Transactions 23, no. 3 (1995): 675–77. http://dx.doi.org/10.1042/bst0230675.

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11

Hashimoto, K., T. Nakanishi, and Y. Kurosawa. "Isolation of carp genes encoding major histocompatibility complex antigens." Proceedings of the National Academy of Sciences 87, no. 17 (1990): 6863–67. http://dx.doi.org/10.1073/pnas.87.17.6863.

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12

KNETEMAN, N. M., P. F. HALLORAN, W. D. SANDEN, T. WANG, and R. E. A. SEELIS. "MAJOR HISTOCOMPATIBILITY COMPLEX ANTIGENS AND MURINE ISLET ALLOGRAFT SURVIVAL." Transplantation 51, no. 1 (1991): 247–51. http://dx.doi.org/10.1097/00007890-199101000-00041.

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13

McEnery, Paul T., and Thomas R. Welch. "Major histocompatibility complex antigens in steroid-responsive nephrotic syndrome." Pediatric Nephrology 3, no. 1 (1989): 33–36. http://dx.doi.org/10.1007/bf00859622.

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14

Longjam, Langamba Angom, and Dipmala Das. "Major histocompatibility complex and its importance towards controlling infection." Asian Journal of Medical Sciences 8, no. 2 (2017): 1–13. http://dx.doi.org/10.3126/ajms.v8i2.16189.

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It is well documented that infectious pathogen burden and infected cell mass determine the clinical severity of infectious diseases, however, the ability of the host to recognize and process antigens to produce antibodies or the cellular immune response during infection could be under genetic control. The Major Histocompatibility Complex (MHC) or Human Leukocyte Antigen (HLA) system is the most intensively studied of all genetic systems because of its influence to many important traits, including resistance to infectious diseases, autoimmunity and immunological self or nonself compatibility. T

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15

Bhayani, H., and Y. Paterson. "Analysis of peptide binding patterns in different major histocompatibility complex/T cell receptor complexes using pigeon cytochrome c-specific T cell hybridomas. Evidence that a single peptide binds major histocompatibility complex in different conformations." Journal of Experimental Medicine 170, no. 5 (1989): 1609–25. http://dx.doi.org/10.1084/jem.170.5.1609.

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The interaction of TCR, antigen, and MHC complex has been analyzed using synthetic peptide antigens and a series of single amino acid-substituted analogues. Two similar antigens, mouse cytochrome c (mcyt c) and pigeon cytochrome c (pcyt c), elicit T cell responses in strains of mice bearing MHC class II Ek beta Ek alpha (B10.A), Eb beta Ek alpha [B10.A(5R)], and Es beta Ek alpha [B10.S(9R)]. The immunogenic regions of these antigens are located in the peptide sequence p88-104 for pcyt c and m88-103 for mcyt c. The limited T cell repertoire for these antigens is comprised of four groups of T ce

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16

van Ham, Marieke, Marcel van Lith, Björn Lillemeier, et al. "Modulation of the Major Histocompatibility Complex Class II–Associated Peptide Repertoire by Human Histocompatibility Leukocyte Antigen (Hla)-Do." Journal of Experimental Medicine 191, no. 7 (2000): 1127–36. http://dx.doi.org/10.1084/jem.191.7.1127.

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Antigen presentation by major histocompatibility complex class II molecules is essential for antibody production and T cell activation. For most class II alleles, peptide binding depends on the catalytic action of human histocompatibility leukocyte antigens (HLA)-DM. HLA-DO is selectively expressed in B cells and impedes the activity of DM, yet its physiological role remains unclear. Cell surface iodination assays and mass spectrometry of major histocompatibility complex class II–eluted peptides show that DO affects the antigenic peptide repertoire of class II. DO generates both quantitative a

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17

Tomita, Yoshihiko. "MAJOR HISTOCOMPATIBILITY COMPLEX CLASS II ANTIGENS ON RENAL CELL CANCER." Japanese Journal of Urology 81, no. 7 (1990): 1079–86. http://dx.doi.org/10.5980/jpnjurol1989.81.1079.

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18

Low, B. G., P. J. Hansen, M. Drost, and K. J. Gogolin-Ewens. "Expression of major histocompatibility complex antigens on the bovine placenta." Reproduction 90, no. 1 (1990): 235–43. http://dx.doi.org/10.1530/jrf.0.0900235.

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19

Li, Xian C., and Malini Raghavan. "Structure and function of major histocompatibility complex class I antigens." Current Opinion in Organ Transplantation 15, no. 4 (2010): 499–504. http://dx.doi.org/10.1097/mot.0b013e32833bfb33.

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20

Banovac, K., Latifa Ghandur-Mnaymneh, J. Leone, D. Neylan, and A. Rabinovitch. "Intrathyroidal Mast Cells Express Major Histocompatibility Complex Class-II Antigens." International Archives of Allergy and Immunology 90, no. 1 (1989): 43–46. http://dx.doi.org/10.1159/000234998.

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21

Skoskiewicz, M. J., R. B. Colvin, E. E. Schneeberger, and P. S. Russell. "Widespread and selective induction of major histocompatibility complex-determined antigens in vivo by gamma interferon." Journal of Experimental Medicine 162, no. 5 (1985): 1645–64. http://dx.doi.org/10.1084/jem.162.5.1645.

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gamma Interferon (IFN-gamma) caused remarkable increases in class I (H-2Kk) and class II (I-Ak) antigens throughout the body by 6-9 d. Heart, kidney, and adrenals showed increases of 4-8 times their previous levels of class I antigen content, while the pancreas and small intestine increased 13-17-fold. Lesser increases were found in spleen, liver, and lung, which showed higher resting antigenic potency. Increases of class II antigenicity of 6-10-fold were found in heart, kidney, pancreas, lung, liver, adrenal, and small intestine, with lesser increases in thymus and spleen, and none in lymph n

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22

Tompkins, S. M., J. C. Moore, and P. E. Jensen. "An insulin peptide that binds an alternative site in class II major histocompatibility complex." Journal of Experimental Medicine 183, no. 3 (1996): 857–66. http://dx.doi.org/10.1084/jem.183.3.857.

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We report that a peptide from the B chain of insulin, B(10-30), binds with high affinity to multiple class II proteins, including IAb,d,k, IEd,k, and DR1. The ability of B(10-30) to inhibit the binding of other peptide antigens to class II does not correlate with its affinity for class II. B(10-30) only weakly inhibits the binding of antigenic peptides. Conversely, peptides with high affinity for the peptide-binding groove of various class II proteins do not inhibit B(10-30) binding. The rate of association of B(10-30) with class II is unusually rapid, approaching saturation in 1-2 h compared

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23

Benichou, G., P. A. Takizawa, P. T. Ho, et al. "Immunogenicity and tolerogenicity of self-major histocompatibility complex peptides." Journal of Experimental Medicine 172, no. 5 (1990): 1341–46. http://dx.doi.org/10.1084/jem.172.5.1341.

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Mechanisms involved in self-antigen processing and presentation are crucial in understanding the induction of self-tolerance in the thymus. We examined the immunogenicity of determinants from major histocompatibility complex (MHC) molecules that are expressed in the thymus and have tested peptides derived from the polymorphic regions of class I and class II molecules. We found that two peptides corresponding to NH2 termini of the class II alpha and beta chains (Ak alpha 1-18 and Ak beta 1-16) could bind to self-Ak molecules with high affinity and, surprisingly, were immunogenic in that they co

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24

De Oliveira Andrade, Luis Jesuino, Paulo Roberto Santana de Melo, Larissa Santos França, Luciana Santos França, Ana Micheline Andrade Malta, and Raymundo Paraná. "Human major histocompatibility complex and thyroid dysfunction in hepatitis C carries." Revista de Ciências Médicas e Biológicas 10, no. 2 (2011): 179. http://dx.doi.org/10.9771/cmbio.v10i2.4825.

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The major histocompatibility complex (MHC) is a multigene family of receptors which are crucial in antigen presentation, mediation, and initiation of the cellular immune response. An association exists between certain MHC polymorphisms and autoimmune thyroid disease in animals and humans. Hepatitis C virus (HCV) infection has been shown to be associated with increased incidence of thyroid dysfunction, moreover, interferon-á (IFN-á) therapy of chronic HCV infection is associated with the thyroid dysfunction. IFN-á has been the basis for the treatment of HCV infection has been identified as an i

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25

Gil-Torregrosa, Beatriz C., A. Raúl Castaño, and Margarita Del Val. "Major Histocompatibility Complex Class I Viral Antigen Processing in the Secretory Pathway Defined by the trans-Golgi Network Protease Furin." Journal of Experimental Medicine 188, no. 6 (1998): 1105–16. http://dx.doi.org/10.1084/jem.188.6.1105.

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Classical antigen presentation by major histocompatibility complex class I molecules involves cytosolic processing of endogenously synthesized antigens by proteasomes and translocation of processed peptides into the endoplasmic reticulum (ER) by transporters associated with antigen presentation (TAP). Alternative pathways for processing of endogenous antigens, generally involving the ER, have been suggested but not fully proved. We analyzed the potential for class I presentation of proteolytic maturation of secretory antigens in the exocytic pathway. We found that hepatitis B (HB) virus secret

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26

Radaelli, E., F. Del Piero, L. Aresu, et al. "Expression of Major Histocompatibility Complex Class II Antigens in Porcine Leptospiral Nephritis." Veterinary Pathology 46, no. 5 (2009): 800–809. http://dx.doi.org/10.1354/vp.08-vp-0078-r-fl.

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Class II major histocompatibility complex (MHCII) is required for the presentation of antigens to CD4 helper T cells. During nephritis, not only primary antigen presenting cells such as histiocytes and lymphocytes, but also cytokine-stimulated tubular epithelial cells express MHCII. Leptospirosis in fattening pigs is characterized by several degrees of nephritis, from absence of lesions to severe multifocal tubulo-interstitial inflammation. Renal tissue from 20 8-month-old pigs with spontaneous nephritis and 6 control pigs without renal lesions were investigated for leptospirosis by indirect i

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27

Woods, A., H. Y. Chen, M. E. Trumbauer, A. Sirotina, R. Cummings, and D. M. Zaller. "Human major histocompatibility complex class II-restricted T cell responses in transgenic mice." Journal of Experimental Medicine 180, no. 1 (1994): 173–81. http://dx.doi.org/10.1084/jem.180.1.173.

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Transgenic mice expressing human major histocompatibility complex (MHC) class II molecules would provide a valuable model system for studying human immunology. However, attempts to obtain human class II-restricted T cell responses in such transgenic mice have had only limited success, possibly due to an inability of mouse CD4 to interact efficiently with human MHC class II molecules. To circumvent this problem, we constructed recombinant MHC class II genes in which the peptide-binding domain was derived from human DR sequences whereas the CD4-binding domain was derived from mouse I-E sequences

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28

Bieberich, C., T. Yoshioka, K. Tanaka, G. Jay, and G. Scangos. "Functional expression of a heterologous major histocompatibility complex class I gene in transgenic mice." Molecular and Cellular Biology 7, no. 11 (1987): 4003–9. http://dx.doi.org/10.1128/mcb.7.11.4003.

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The regulated expression of major histocompatibility complex class I antigens is essential for assuring proper cellular immune responses. To study H-2 class I gene regulation, we have transferred a foreign class I gene to inbred mice and have previously shown that the heterologous class I gene was expressed in a tissue-dependent manner. In this report, we demonstrate that these mice expressed the transgenic class I molecule on the cell surface without any alteration in the level of endogenous H-2 class I antigens. Skin grafts from transgenic mice were rapidly rejected by mice of the background

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29

Bieberich, C., T. Yoshioka, K. Tanaka, G. Jay, and G. Scangos. "Functional expression of a heterologous major histocompatibility complex class I gene in transgenic mice." Molecular and Cellular Biology 7, no. 11 (1987): 4003–9. http://dx.doi.org/10.1128/mcb.7.11.4003-4009.1987.

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The regulated expression of major histocompatibility complex class I antigens is essential for assuring proper cellular immune responses. To study H-2 class I gene regulation, we have transferred a foreign class I gene to inbred mice and have previously shown that the heterologous class I gene was expressed in a tissue-dependent manner. In this report, we demonstrate that these mice expressed the transgenic class I molecule on the cell surface without any alteration in the level of endogenous H-2 class I antigens. Skin grafts from transgenic mice were rapidly rejected by mice of the background

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30

BRILES, W. E., and RUTH W. BRILES. "Genetics and Classification of Major Histocompatibility Complex Antigens of the Chicken." Poultry Science 66, no. 5 (1987): 776–81. http://dx.doi.org/10.3382/ps.0660776.

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31

Schust, Danny J., Domenico Tortorella, and Hidde L. Ploegh. "Viral immunoevasive strategies and trophoblast class I major histocompatibility complex antigens." Journal of Reproductive Immunology 43, no. 2 (1999): 243–51. http://dx.doi.org/10.1016/s0165-0378(99)00024-8.

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32

Bharadwaj, Mandvi, Patricia Illing, Alex Theodossis, Anthony W. Purcell, Jamie Rossjohn, and James McCluskey. "Drug Hypersensitivity and Human Leukocyte Antigens of the Major Histocompatibility Complex." Annual Review of Pharmacology and Toxicology 52, no. 1 (2012): 401–31. http://dx.doi.org/10.1146/annurev-pharmtox-010611-134701.

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33

Hultman, C. Scott, John P. Hunt, Hiromasa Yamamoto, et al. "Immunogenicity of Cultured Keratinocyte Allografts Deficient in Major Histocompatibility Complex Antigens." Journal of Trauma: Injury, Infection, and Critical Care 45, no. 1 (1998): 25–34. http://dx.doi.org/10.1097/00005373-199807000-00005.

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34

Markey, A. C., L. J. Churchill, and D. M. MacDonald. "Altered expression of major histocompatibility complex (MHC) antigens by epidermal tumours." Journal of Cutaneous Pathology 17, no. 2 (1990): 65–71. http://dx.doi.org/10.1111/j.1600-0560.1990.tb00058.x.

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35

Simister, Neil E. "IgG Fe receptors that resemble class I major histocompatibility complex antigens." Biochemical Society Transactions 21, no. 4 (1993): 973–76. http://dx.doi.org/10.1042/bst0210973.

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36

PICCININI, L. A., S. H. ROMAN, and T. F. DAVIES. "AUTOIMMUNE THYROIDDISEASE AND THYROID CELL CLASS II MAJOR HISTOCOMPATIBILITY COMPLEX ANTIGENS." Clinical Endocrinology 26, no. 2 (1987): 253–72. http://dx.doi.org/10.1111/j.1365-2265.1987.tb00783.x.

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37

Misra, D. N., H. W. Kunz, and T. J. Gill, III. "Beta-2-Microglobulin of Rat Major Histocompatibility Complex Class I Antigens." International Archives of Allergy and Immunology 89, no. 2-3 (1989): 120–27. http://dx.doi.org/10.1159/000234934.

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38

SAITO, MITSURU, DHIRENDRA N. MISRA, HEINZ W. KUNZ, and THOMAS J. GILL. "Major Histocompatibility Complex Class I Antigens Expressed on Rat Trophoblast Cells." American Journal of Reproductive Immunology 22, no. 1-2 (1990): 26–32. http://dx.doi.org/10.1111/j.1600-0897.1990.tb01028.x.

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39

Yu, Leonard T., Abdolmohammad Rostami, Wilys K. Silvers, Don Larossa, and William F. Hickey. "Expression of major histocompatibility complex antigens on inflammatory peripheral nerve lesions." Journal of Neuroimmunology 30, no. 2-3 (1990): 121–28. http://dx.doi.org/10.1016/0165-5728(90)90095-5.

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40

Gores, Gregory J., S. Breanndan Moore, Lloyd D. Fisher, Frank C. Powell, and E. Rolland Dickson. "Primary biliary cirrhosis: Associations with class II major histocompatibility complex antigens." Hepatology 7, no. 5 (1987): 889–92. http://dx.doi.org/10.1002/hep.1840070516.

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41

Tanaka, K., E. Gorelik, M. Watanabe, N. Hozumi, and G. Jay. "Rejection of B16 melanoma induced by expression of a transfected major histocompatibility complex class I gene." Molecular and Cellular Biology 8, no. 4 (1988): 1857–61. http://dx.doi.org/10.1128/mcb.8.4.1857.

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Transfection of a functional major histocompatibility complex class I gene into certain tumor cells, induced by oncogenic viruses or chemical carcinogens, can effectively abrogate their tumorigenic activity. Since experimentally induced tumors possess strong tumor-specific transplantation antigens, expression of cell surface class I antigens may present the tumor cells to appropriate immune effector cells. Most spontaneously arising tumors do not possess tumor-specific transplantation antigens, and their tumorigenicity may not be affected by the expression of a transfected class I gene. We dem

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42

Tanaka, K., E. Gorelik, M. Watanabe, N. Hozumi, and G. Jay. "Rejection of B16 melanoma induced by expression of a transfected major histocompatibility complex class I gene." Molecular and Cellular Biology 8, no. 4 (1988): 1857–61. http://dx.doi.org/10.1128/mcb.8.4.1857-1861.1988.

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Transfection of a functional major histocompatibility complex class I gene into certain tumor cells, induced by oncogenic viruses or chemical carcinogens, can effectively abrogate their tumorigenic activity. Since experimentally induced tumors possess strong tumor-specific transplantation antigens, expression of cell surface class I antigens may present the tumor cells to appropriate immune effector cells. Most spontaneously arising tumors do not possess tumor-specific transplantation antigens, and their tumorigenicity may not be affected by the expression of a transfected class I gene. We dem

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43

Milligan, G. N., L. Flaherty, V. L. Braciale, and T. J. Braciale. "Nonconventional (TL-encoded) major histocompatibility complex molecules present processed viral antigen to cytotoxic T lymphocytes." Journal of Experimental Medicine 174, no. 1 (1991): 133–38. http://dx.doi.org/10.1084/jem.174.1.133.

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A large number of class I-like genes are located distal to the K and D regions of the murine major histocompatibility complex (MHC) within the Q and TL region. The function of the molecules encoded within this region is obscure since unlike conventional MHC gene products, these molecules have not been reported to present processed environmental antigens to T cells. In the present report, we demonstrate that a peptide corresponding to processed influenza virus hemagglutinin can be recognized by CD8+ T cell receptor alpha/beta-positive cytotoxic T lymphocytes (CTL) in association with a MHC clas

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44

Lankar, Danielle, Volker Briken, Kristin Adler та ін. "Syk Tyrosine Kinase and B Cell Antigen Receptor (BCR) Immunoglobulin-α Subunit Determine BCR-mediated Major Histocompatibility Complex Class II–restricted Antigen Presentation". Journal of Experimental Medicine 188, № 5 (1998): 819–31. http://dx.doi.org/10.1084/jem.188.5.819.

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Stimulation of CD4+ helper T lymphocytes by antigen-presenting cells requires the degradation of exogenous antigens into antigenic peptides which associate with major histocompatibility complex (MHC) class II molecules in endosomal or lysosomal compartments. B lymphocytes mediate efficient antigen presentation first by capturing soluble antigens through clonally distributed antigen receptors (BCRs), composed of membrane immunoglobulin (Ig) associated with Ig-α/Ig-β heterodimers which, second, target antigens to MHC class II–containing compartments. We report that antigen internalization and an

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45

Clement, Loran T. "The Class II Major Histocompatibility Complex Antigen Deficiency Syndrome: Consequences of Absent Class II Major Histocompatibility Antigens for Lymphocyte Differentiation and Function." Journal of Investigative Dermatology 94, no. 6 (1990): s118—s121. http://dx.doi.org/10.1111/1523-1747.ep12876078.

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46

Siegrist, C. A., E. Martinez-Soria, I. Kern, and B. Mach. "A novel antigen-processing-defective phenotype in major histocompatibility complex class II-positive CIITA transfectants is corrected by interferon-gamma." Journal of Experimental Medicine 182, no. 6 (1995): 1793–99. http://dx.doi.org/10.1084/jem.182.6.1793.

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Presentation of exogenous protein antigens to T lymphocytes is based on the intersection of two complex pathways: (a) synthesis, assembly, and transport of major histocompatibility complex (MHC) class II-invariant chain complexes from the endoplasmic reticulum to a specialized endosomal compartment, and (b) endocytosis, denaturation, and proteolysis of antigens followed by loading of antigenic peptides onto newly synthesized MHC class II molecules. It is believed that expression of MHC class II heterodimers, invariant chain and human leukocyte antigen-DM is both necessary and sufficient to rec

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47

Uyenoyama, M. K. "Coevolution of the major histocompatibility complex and the t-complex in the mouse. I. Generation and maintenance of high complementarity associations." Genetics 121, no. 1 (1989): 139–51. http://dx.doi.org/10.1093/genetics/121.1.139.

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Abstract A quantitative model is developed to explore the effects of prezygotic and postzygotic incompatibility on the origin and maintenance of associations between the major histocompatibility complex (MHC) and the t-complex in the mouse. Incompatibility is represented by a reduction in the rate of conception or gestation of offspring derived from sperm bearing MHC antigens in common with the mother. Incompatibility encourages the evolution of associations from a state of complete independence between the two complexes by promoting the invasion of all novel antigens, including those that exh

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48

Sharma, Preeti, Pradeep Kumar, and Rachna Sharma. "THE MAJOR HISTOCOMPATIBILITY COMPLEX: A REVIEW." Asian Journal of Pharmaceutical and Clinical Research 10, no. 2 (2017): 33. http://dx.doi.org/10.22159/ajpcr.2017.v10i2.15555.

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One of the important components of the immune system, the major histocompatibility complex (MHC) molecules allow T-lymphocytes to detect cells, such as macrophages, B-lymphocytes, and dendritic cells that ingest infectious microorganisms or the self-cells infected with microorganism. On being engulfed a microorganism, macrophage partially digests it and displays peptide fragments of the microbe on its surface, bound to MHC molecules and the T-lymphocyte recognizes the foreign fragment attached to the MHC molecule and binds to it, lead to stimulation of an immune response. The MHC molecule pres

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49

Neild, Annie, Takahiro Murata, and Craig R. Roy. "Processing and Major Histocompatibility Complex Class II Presentation of Legionella pneumophila Antigens by Infected Macrophages." Infection and Immunity 73, no. 4 (2005): 2336–43. http://dx.doi.org/10.1128/iai.73.4.2336-2343.2005.

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ABSTRACT To better understand interactions between the intracellular pathogen Legionella pneumophila and macrophages (Mφs), host and bacterial determinants important for presentation of antigens on major histocompatibility complex class II molecules (MHC-II) were investigated. It was determined that immune CD4 T-cell responses to murine bone marrow-derived Mφs (BMφs) infected with wild-type L. pneumophila were higher than the responses to avirulent dotA mutant bacteria. Although this enhanced response by immune T cells required modulation of vacuole transport mediated by the Dot/Icm system, it

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50

Warrens, Anthony N. "Studies on the Interaction of T-Cells with Major Histocompatibility Complex Class II Antigens." Clinical Science 92, no. 1 (1997): 25–36. http://dx.doi.org/10.1042/cs0920025.

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1. Major histocompatibility complex class II antigens have the central role in the immune response of ‘presenting’ antigenic peptide to CD4+ T-cells. This interaction with a T-cell's receptor may result in activation, but, if recognition occurs without collateral molecular interactions which cause ‘co-stimulation’, these T-cells will be tolerized. 2. In the light of current interest in muscle cell transplantation, a transformed myoblast, TE671, phenotypically comparable to untransformed cells, transfected to express class II, was studied as a stable model of antigen presentation by muscle cell

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