Abstract: We have identified and extensively characterized a type IV collagen alpha chain, referred to as alpha 5(IV). Four overlapping cDNA clones isolated contain an open reading frame for 543 amino acid residues of the carboxyl-terminal end of a collagenous domain, a 229-residue carboxyl-terminal noncollagenous domain, and 1201 base pairs coding for a 3' untranslated region. The collagenous Gly-Xaa-Yaa repeat sequence has five imperfections that coincide with those in the corresponding region of the alpha 1(IV) chain. The noncollagenous domain has 12 conserved cysteine residues and 83% and 63% sequence identity with the noncollagenous domains of the alpha 1(IV) and alpha 2(IV) chains, respectively. The alpha 5(IV) chain has less sequence identity with the putative bovine alpha 3(IV) and alpha 4(IV) chains. Antiserum against an alpha 5(IV) synthetic peptide stained a polypeptide chain of about 185 kDa by immunoblot analysis and immunolocalization of the chain in human kidney was almost completely restricted to the glomerulus. The gene was assigned to the Xq22 locus by somatic cell hybrids and in situ hybridization. This may be identical or close to the locus of the X chromosome-linked Alport syndrome that is believed to be a type IV collagen disease.

Abstract: The social development of a female rhesus monkey (Macaca mulatta) was followed from the day of birth until her death, at age 32 months. The subject, born to an older mother, had an extra autosome (karyotype: 43, XX, +18), an affliction that came about spontaneously. MRI scans revealed that she was also hydrocephalic. Compared to 23 female monkeys growing up under identical conditions, the subject showed serious motor deficiencies, a dramatic delay in the development of social behavior, poorly established dominance relationships, and greater than usual dependency on mother and kin. The subject was well-integrated into the social group, however.