[Inhibition of adjuvant-arthritis with lathyrism].
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Animals↗
Biomedical subjects
R Timpl
Publications and source records attributed to R Timpl.
[Studies on the specific reaction ranges of collagen antigens. I. Demonstration of the specific reaction of low-molecular collagen peptides with antiserums against native and denatured soluble collagen].
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Antigen-Antibody Reactions↗
The J1 glycoprotein--a novel nervous system cell adhesion molecule of the L2/HNK-1 family.
The neural cell adhesion molecules L1 and N-CAM share a common carbohydrate epitope that is recognized by the monoclonal antibodies L2 and HNK-1. The L2/HNK-1 epitope is also present on the myelin-associated glycoprotein (MAG) which is thought to mediate surface interactions between the axon and myelinating cell. Other, as yet unidentified, cell-surface glycoproteins are recognized by the two antibodies and are believed to belong to a family of neural cell adhesion molecules. To test this hypothesis, we have prepared polyclonal antibodies to a prominent member of the L2/HNK-1 family, the 160K (relative molecular mass (Mr)160,000) glycoprotein. Here we report that these antibodies, designated J1 antibodies, react with astrocytes and oligodendrocytes and interfere with neurone-astrocyte adhesion, but not with neurone-neurone or astrocyte-astrocyte adhesion. This result suggests the involvement of the J1 antigen in cell-cell interactions.
Animals↗
The aminopropeptide of collagen.
Aminopropeptides are triple-standard structures with a molecular weight of about 40,000-45,000 located at the amino end of procollagens. They are released during the conversion of procollagen into collagen by specific proteases cleaving a single Pro-Gln peptide bond. The individual peptide chains usually consist of a compact noncollagenous domain stabilized by intrachain disulfide bridges and a collagenous domain folded into a triple helix. Chemical and immunologic analyses of different types of procollagen have demonstrated certain sequence homologies but also distinct structural differences between their aminopropeptides. These peptides may be involved in the control of collagen synthesis and fibril formation. Some inherited disorders (dermatosparaxis, Ehlers-Danlos syndrome Type VII) are characterized by an incomplete release of the aminopropeptide in situ. Immunologic reagents have been developed which also allow the study of aminopropeptide metabolism in a variety of acquired connective tissue diseases.
Amino Acid Sequence↗