IDENTIFICATION OF I-PLASTIN, A HUMAN FIMBRIN ISOFORM EXPRESSED IN INTESTINE AND KIDNEY

被引:91
作者
LIN, CS
SHEN, WY
CHEN, ZP
TU, YH
MATSUDAIRA, P
机构
[1] MIT,WHITEHEAD INST,CAMBRIDGE,MA 02139
[2] MIT,DEPT BIOL,CAMBRIDGE,MA 02139
[3] PALO ALTO MED FDN,RES INST,PALO ALTO,CA 94301
关键词
D O I
10.1128/MCB.14.4.2457
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The complete cDNA sequence of human intestine-specific plastin (I-plastin) was determined from a clone derived by PCR. It consists of a 97-bp 5' untranslated region, a 1,887-bp coding region, and a 1,655-bp 3' untranslated region. The coding region predicts a 629-residue polypeptide whose sequence displays 86, 75, and 73% identities with chicken intestine fimbrin, human T-plastin, and human L-plastin, respectively. Recombinant I-plastin cross-linked actin filaments into bundles in the absence but not in the presence of calcium. The I-plastin gene was mapped by PCR to human chromosome 3; the L- and T-plastin genes were previously mapped to chromosomes 13 and X, respectively. I-plastin mRNA was detected in the small intestine, colon, and kidneys; relatively lower levels of expression were detected in the lungs and stomach. In contrast, L-plastin expression was restricted to the spleen and other lymph node-containing organs, while T-plastin was expressed in a variety of organs, including muscle, brain, uterus, and esophagus. In contrast to the situation for the intestine, high levels of L- and T-plastin mRNAs were detected in Caco-2, a human colon-derived cell line. Immunofluorescence microscopy detected I-plastin in the brush border of the small intestine and colon. These results identify I-plastin as the human homolog of chicken intestine fimbrin and as a third plastin isoform in humans.
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页码:2457 / 2467
页数:11
相关论文
共 28 条
[1]   REQUIREMENT OF YEAST FIMBRIN FOR ACTIN ORGANIZATION AND MORPHOGENESIS INVIVO [J].
ADAMS, AEM ;
BOTSTEIN, D ;
DRUBIN, DG .
NATURE, 1991, 354 (6352) :404-408
[2]  
ANDERSON NL, 1985, CANCER RES, V45, P4955
[4]   MOLECULAR-BASIS FOR THE INFLUENCE OF MUSCLE LENGTH ON MYOCARDIAL PERFORMANCE [J].
BABU, A ;
SONNENBLICK, E ;
GULATI, J .
SCIENCE, 1988, 240 (4848) :74-76
[5]   VILLIN SEQUENCE AND PEPTIDE MAP IDENTIFY 6 HOMOLOGOUS DOMAINS [J].
BAZARI, WL ;
MATSUDAIRA, P ;
WALLEK, M ;
SMEAL, T ;
JAKES, R ;
AHMED, Y .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1988, 85 (14) :4986-4990
[6]   FIMBRIN, A NEW MICROFILAMENT-ASSOCIATED PROTEIN PRESENT IN MICROVILLI AND OTHER CELL-SURFACE STRUCTURES [J].
BRETSCHER, A ;
WEBER, K .
JOURNAL OF CELL BIOLOGY, 1980, 86 (01) :335-340
[7]   ISOLATION OF BIOLOGICALLY-ACTIVE RIBONUCLEIC-ACID FROM SOURCES ENRICHED IN RIBONUCLEASE [J].
CHIRGWIN, JM ;
PRZYBYLA, AE ;
MACDONALD, RJ ;
RUTTER, WJ .
BIOCHEMISTRY, 1979, 18 (24) :5294-5299
[8]   FIMBRIN IS A HOMOLOG OF THE CYTOPLASMIC PHOSPHOPROTEIN PLASTIN AND HAS DOMAINS HOMOLOGOUS WITH CALMODULIN AND ACTIN GELATION PROTEINS [J].
DEARRUDA, MV ;
WATSON, S ;
LIN, CS ;
LEAVITT, J ;
MATSUDAIRA, P .
JOURNAL OF CELL BIOLOGY, 1990, 111 (03) :1069-1079
[9]  
EZZELL RM, 1989, DEVELOPMENT, V106, P407
[10]  
GLENNEY JR, 1981, J BIOL CHEM, V256, P9283