{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T16:40:11Z","timestamp":1781109611698,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"8","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1988,4]]},"abstract":"<jats:p>The cell-surface glycoprotein Mo1 is a member of the family of leukocyte cell adhesion molecules (Leu-CAMs) that includes lymphocyte function-associated antigen 1 (LFA-1) and p150,95. Each Leu-CAM is a heterodimer with a distinct alpha subunit noncovalently associated with a common beta subunit. Leu-CAMs play crucial roles in cell-cell and cell-matrix interactions. We describe the isolation and analysis of two partial cDNA clones encoding the alpha subunit of the Leu-CAM Mo1 in humans and guinea pigs. A monoclonal antibody directed against an epitope in the carboxyl-terminal portion of the guinea pig alpha chain was used for immunoscreening a lambda gt11 expression library. The sequence of a 378-base-pair insert from one immunoreactive clone revealed a single continuous open reading frame encoding 126 amino acids including a 26-amino acid tryptic peptide isolated from the purified guinea pig alpha subunit. A cDNA clone of identical size was isolated from a human monocyte\/lymphocyte cDNA library by using the guinea pig clone as a probe. The human clone also encoded a 126-amino acid peptide including the sequence of an additional tryptic peptide present in purified human Mo1 alpha chain. RNA gel blots revealed that mature Mo1 alpha chain mRNA is approximately 5 kilobases in guinea pigs and humans. Southern analysis of DNA from hamster-human hybrids localized the human Mo1 alpha chain to chromosome 16, which has been shown to contain the gene for the alpha chain of lymphocyte function-associated antigen 1. A comparison of the Mo1 alpha chain coding region revealed significant homologies with carboxyl-terminal portions of the alpha subunits of fibronectin, vitronectin, and platelet IIb\/IIIa receptors. These data suggest that the alpha subunits of Leu-CAMs evolved by gene duplication from a common ancestral gene and strengthen the hypothesis that the alpha subunits of these heterodimeric cell adhesion molecules on myeloid and lymphoid cells, platelets, and fibroblasts are evolutionary related.<\/jats:p>","DOI":"10.1073\/pnas.85.8.2776","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T06:53:09Z","timestamp":1149058389000},"page":"2776-2780","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":19,"title":["Molecular cloning of the alpha subunit of human and guinea pig leukocyte adhesion glycoprotein Mo1: chromosomal localization and homology to the alpha subunits of integrins."],"prefix":"10.1073","volume":"85","author":[{"given":"M A","family":"Arnaout","sequence":"first","affiliation":[{"name":"Renal Division, Children's Hospital, Boston, MA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"E","family":"Remold-O'Donnell","sequence":"additional","affiliation":[{"name":"Renal Division, Children's Hospital, Boston, MA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M W","family":"Pierce","sequence":"additional","affiliation":[{"name":"Renal Division, Children's Hospital, Boston, MA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P","family":"Harris","sequence":"additional","affiliation":[{"name":"Renal Division, Children's Hospital, Boston, MA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D G","family":"Tenen","sequence":"additional","affiliation":[{"name":"Renal Division, Children's Hospital, Boston, MA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1988,4]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.85.8.2776","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T12:46:23Z","timestamp":1649853983000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.85.8.2776"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1988,4]]},"references-count":0,"journal-issue":{"issue":"8","published-print":{"date-parts":[[1988,4]]}},"alternative-id":["10.1073\/pnas.85.8.2776"],"URL":"https:\/\/doi.org\/10.1073\/pnas.85.8.2776","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1988,4]]},"assertion":[{"value":"1988-04-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}