Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-1-21
pubmed:databankReference
pubmed:abstractText
Squamous cell carcinoma antigens (SCCA) 1 and 2 are inhibitory members of the high-molecular-weight serine proteinase inhibitor (serpin) family. The biological functions of SCCA1 and 2 are unknown. One approach to determining the function of human proteins is to study orthologs in other species, such as the mouse. The purpose of this study was to determine whether orthologs to human SCCA1 or 2 exist in the mouse. We report the identification and characterization of a novel serpin, sqn5 (now designated Scca2). Comparative amino acid sequence analysis suggests that Scca2 is a member of the ov-serpin subfamily of serpins with highest homology to SCCA1 and SCCA2. Fluorescence in situ hybridization revealed that the Scca2 mapped near Bcl2 on mouse chromosome 1. This region is syntenic with the human locus for SCCA1 and SCCA2 on 18q21.3. The tissue expression patterns as determined by RT-PCR showed a restricted distribution. Scca2 was detected in the lung, thymus, skin, and uterus, as are SCCA1 and SCCA2. Unlike the SCCAs, however, Scca2 was detected also in the gastrointestinal tract. Enzyme-inhibition assays using a GST-SCCA2 fusion protein revealed that SCCA2 inhibited chymotrypsin-like serine proteinases, but not papain-like cysteine proteinases. SCCA2 inhibited CTSG at 1:1 stoichiometry and with a second-order rate constant of kass = 1.7 x 10(5) M-1 s-1. SCCA2 also inhibited human mast cell chymase but the stoichiometry was 2:1, and the second-order rate constant was kass = 0.9 x 10(4) M-1 s-1. This inhibitory profile is identical to that observed for human SCCA2. Based on these findings, Scca2 appears to be the murine ortholog of human SCCA2.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0888-7543
pubmed:author
pubmed:copyrightInfo
Copyright 1998 Academic Press.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
297-306
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9828132-Amino Acid Sequence, pubmed-meshheading:9828132-Animals, pubmed-meshheading:9828132-Antigens, Neoplasm, pubmed-meshheading:9828132-Base Sequence, pubmed-meshheading:9828132-Chromosome Mapping, pubmed-meshheading:9828132-Chromosomes, Human, Pair 1, pubmed-meshheading:9828132-Chymases, pubmed-meshheading:9828132-Cloning, Molecular, pubmed-meshheading:9828132-Conserved Sequence, pubmed-meshheading:9828132-Humans, pubmed-meshheading:9828132-In Situ Hybridization, Fluorescence, pubmed-meshheading:9828132-Kinetics, pubmed-meshheading:9828132-Mice, pubmed-meshheading:9828132-Molecular Sequence Data, pubmed-meshheading:9828132-Promoter Regions, Genetic, pubmed-meshheading:9828132-RNA, Messenger, pubmed-meshheading:9828132-Recombinant Fusion Proteins, pubmed-meshheading:9828132-Restriction Mapping, pubmed-meshheading:9828132-Sequence Alignment, pubmed-meshheading:9828132-Sequence Analysis, DNA, pubmed-meshheading:9828132-Serine Endopeptidases, pubmed-meshheading:9828132-Serine Proteinase Inhibitors, pubmed-meshheading:9828132-Serpins
pubmed:year
1998
pubmed:articleTitle
A murine ortholog of the human serpin SCCA2 maps to chromosome 1 and inhibits chymotrypsin-like serine proteinases.
pubmed:affiliation
Department of Pediatrics, Harvard Medical School, Children's Hospital, 300 Longwood Avenue, Boston, Massachusetts, 02115, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't