Identification of two structural types of calcium-dependent adhesion molecules in the chicken embryo.
By using an immunological and peptide mapping approach two calcium-dependent cell-cell adhesion molecules (calCAMs) in the embryonic chicken are compared. A third closely related molecule is identified and compared to the two calCAMs. One of the calCAMs appears to be identical to the previously identified adhesion molecule N-cadherin, originally identified in chicken retina and localized to neural tissues. The second is the same as L-CAM, originally identified in chicken liver but localized to a variety of epithelial tissues. The third, also found in liver, is similar to L-CAM but is much closer in structure to N-cadherin. It is, however, immunologically distinct from N-cadherin. We therefore refer to this newly identified molecule as CRM-L for cadherin-related molecule in liver. CRM-L, N-cadherin, and L-CAM are all cell-surface proteins with a similar stability to tryptic digestion in the presence of calcium. CRM-L has the same molecular mass and isoelectric point as N-cadherin but is distinct from L-CAM in these properties. Two-dimensional peptide maps of complete tryptic digests reveal that CRM-L shares 69% of its peptides with N-cadherin and 20% with L-CAM. On the basis of these data, we suggest that there are at least two distinguishable types of calCAMs in the chicken embryo: one represented by the closely related molecules N-cadherin and CRM-L, and another represented by L-CAM.
Crittenden
S L
SL
University of Wisconsin, Department of Zoology, Madison 53706.
Rutishauser
U
U
Lilien
J
J
D000818:Animals; D000911:Antibodies, Monoclonal; D000954:Antigens, Surface / Q000032:analysis*; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules; D002642:Chick Embryo / Q000502:physiology*; D008099:Liver / Q000196:embryology*; D009928:Organ Specificity; D010449:Peptide Mapping
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface; D015815:Cell Adhesion Molecules