Detection of a common polypeptide chain in I-A and I-E sub-region immunoprecipitates

Jones, Patricia P.; Murphy, Donal B.; Hewgill, Derek; McDevitt, Hugh O.

doi:10.1016/0161-5890(79)90027-0

Cited by 201 publications

(102 citation statements)

References 13 publications

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“…Early studies of immunoprecipitated Ia molecules indicated that both the I-A and I-E subregion products consist of genetically polymorphic glycoprotein heterodimers composed ofa 33-35-kdalton chain, and a 25-27-kdalton /3 chain (18). Later studies by Jones et al (31) documented that a third protein, termed invariant chain because of its nonpolymorphic nature, was also present in anti-Ia immunoprecipitates. Although invariant chain associates specifically with Ia antigens, recent data indicate that the gene controlling this protein lies outside the major histocompatibility complex (32,33).…”

Section: Discussionmentioning

confidence: 99%

Identification of a new component in the murine Ia molecular complex.

Sant¹,

Schwartz²,

Cullen³

1983

The Journal of Experimental Medicine

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In this report, we describe a previously unidentified component in the murine Ia antigen complex. SDS-PAGE analysis of anti-Ia immunoprecipitates prepared from spleen cells biosynthetically labeled with 35S-sulfate showed no detectable incorporation of 35SO4 into alpha, beta, or Ii chains but did not reveal the presence of a novel sulfate-bearing molecule of considerable molecular weight heterogeneity (46-69-kdaltons). The 46-69-kdalton molecule could be precipitated with monoclonal antibodies specific for I-A, I-E, and Ii glycoproteins but was not seen in control precipitates, nor in association with IgG or class I MHC molecules. Preliminary biochemical characterization indicated that the 46-69-kdalton product is extremely polydisperse, both in charge and apparent molecular weight, is sensitive to proteases, and bears the sulfate moiety on a large pronase-resistant structure. These results suggested this component might be a proteoglycan. Definitive identification of this component as a proteoglycan was accomplished by selective enzymatic degradation experiments which showed that the sulfate-bearing component of the 46-69-kdalton molecule is chondroitin 6-sulfate.

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Section: Discussionmentioning

confidence: 99%

Identification of a new component in the murine Ia molecular complex.

Sant¹,

Schwartz²,

Cullen³

1983

The Journal of Experimental Medicine

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“…In any case, MHCII -Ii must pass transferrin receptor-positive early endosomes to reach subsequent endocytic compartments where antigen loading occurs (Benaroch et al 1995;Pond and Watts 1999). In endosomes, MHCII is loaded with peptides only after Ii is degraded by proteolysis (Jones et al 1979;Owen et al 1981;Charron et al 1983;Rudd et al 1985;Cresswell 1990, 1991;Teyton et al 1990). Ii is degraded by multiple proteases in defined sequential cleavage steps, starting at the carboxy-terminal luminal domain, until only the CLIP fragment is left, still occupying the peptide-binding groove of MHCII (Hsing and Rudensky 2005).…”

Section: Biosynthesis Of Mhciimentioning

confidence: 99%

MHC Class II Antigen Presentation by Dendritic Cells Regulated through Endosomal Sorting

Broeke

Wubbolts

Stoorvogel

2013

Cold Spring Harbor Perspectives in Biology

142

102

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For the initiation of adaptive immune responses, dendritic cells present antigenic peptides in association with major histocompatibility complex class II (MHCII) to naïve CD4 þ T lymphocytes. In this review, we discuss how antigen presentation is regulated through intracellular processing and trafficking of MHCII. Newly synthesized MHCII is chaperoned by the invariant chain to endosomes, where peptides from endocytosed pathogens can bind. In nonactivated dendritic cells, peptide-loaded MHCII is ubiquitinated and consequently sorted by the ESCRT machinery to intraluminal vesicles of multivesicular bodies, ultimately leading to lysosomal degradation. Ubiquitination of newly synthesized MHCII is blocked when dendritic cells are activated, now allowing its transfer to the cell surface. This mode of regulation for MHCII is a prime example of how molecular processing and sorting at multivesicular bodies can determine the expression of signaling receptors at the plasma membrane.

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“…Immunoprecipitation studies of biosynthetically labeled MHC-1l molecules have revealed a nonpolymorphic "invariant" chain of 34 000 Da associated with the polymorphic a and fi chains (Jones et al, 1978). Invariant chain associates with nascent MHC-11 molecules until they are transported to a protease-containing endosomal compartment, where it is proteolytically cleaved and dissociates from MHC-11 (Blum and Cresswell, 1988).…”

Section: Mhc-1 Function and Cd8+ T Lymphocytesmentioning

confidence: 99%