Immunohistochemistry of carbonic anhydrase isozyme IX (MN/CA IX) in human gut reveals polarized expression in the epithelial cells with the highest proliferative capacity

被引:135
作者
Saarnio, J
Parkkila, S
Parkkila, AK
Waheed, A
Casey, MC
Zhou, XY
Pastoreková, S
Pastorek, J
Karttunen, T
Haukipuro, K
Kairaluoma, MI
Sly, WS
机构
[1] St Louis Univ, Sch Med, Edward A Doisy Dept Biochem & Mol Biol, St Louis, MO 63104 USA
[2] Oulu Univ, Dept Surg, Oulu, Finland
[3] Oulu Univ, Dept Anat, Oulu, Finland
[4] Oulu Univ, Dept Pathol, Oulu, Finland
[5] Slovak Acad Sci, Inst Virol, Bratislava, Slovakia
关键词
carbonic anhydrase; gastrointestinal; gut; human; immunohistochemistry; intestine; plasma membrane;
D O I
10.1177/002215549804600409
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
MN/CA IX is a recently discovered member of the carbonic anhydrase (CA) gene family that has been identified in the plasma membranes of certain tumor and epithelial cells and found to promote cell proliferation when transfected into NIH3T3 cells. This study presents localization of MN/CA IX in human gut and compares its distribution to those of CA I, II, and IV, which are known to be expressed in the intestinal epithelium. The specificity of the monoclonal antibody for MN/CA IX was confirmed by Western blots and immunostaining of COS-7 cells transfected with MN/CA IX cDNA. Immunohistochemical stainings of human gut revealed prominent polarized staining for MN/CA IX in the basolateral surfaces of the enterocytes of duodenum and jejunum, the reaction being most intense in the crypts. A moderate reaction was also seen in the crypts of ileal mucosa, whereas the staining became generally weaker in the large intestine. The results indicate isozyme-specific regulation of MN/CA IX expression along the cranial-caudal axis of the human gut and place the protein at the sites of rapid cell proliferation. The unique localization of MN/CA IX on the basolateral surfaces of proliferating crypt enterocytes suggests that it might serve as a ligand or a receptor for another protein that regulates intercellular communication or cell proliferation. Furthermore, MN/CA IX has a completely conserved active site domain of CAs suggesting that it could also participate in carbon dioxide/bicarbonate homeostasis.
引用
收藏
页码:497 / 504
页数:8
相关论文
共 40 条
[1]  
BARNEA G, 1994, J BIOL CHEM, V269, P14349
[2]   IDENTIFICATION OF A CARBONIC ANHYDRASE-LIKE DOMAIN IN THE EXTRACELLULAR REGION OF RPTP-GAMMA DEFINES A NEW SUBFAMILY OF RECEPTOR TYROSINE PHOSPHATASES [J].
BARNEA, G ;
SILVENNOINEN, O ;
SHAANAN, B ;
HONEGGER, AM ;
CANOLL, PD ;
DEUSTACHIO, P ;
MORSE, B ;
LEVY, JB ;
LAFORGIA, S ;
HUEBNER, K ;
MUSACCHIO, JM ;
SAP, J ;
SCHLESSINGER, J .
MOLECULAR AND CELLULAR BIOLOGY, 1993, 13 (03) :1497-1506
[3]   CLOSE SIMILARITY BETWEEN RECEPTOR-LINKED TYROSINE PHOSPHATASE AND RAT-BRAIN PROTEOGLYCAN [J].
BARNEA, G ;
GRUMET, M ;
SAP, J ;
MARGOLIS, RU ;
SCHLESSINGER, J .
CELL, 1994, 76 (02) :205-205
[4]   Carbonic anhydrase IV expression in rat and human gastrointestinal tract regional, cellular, and subcellular localization [J].
Fleming, RE ;
Parkkila, S ;
Parkkila, AK ;
Rajaniemi, H ;
Waheed, A ;
Sly, WS .
JOURNAL OF CLINICAL INVESTIGATION, 1995, 96 (06) :2907-2913
[5]   STUDIES OF INTESTINAL STEM-CELLS USING NORMAL, CHIMERIC, AND TRANSGENIC MICE [J].
GORDON, JI ;
SCHMIDT, GH ;
ROTH, KA .
FASEB JOURNAL, 1992, 6 (12) :3039-3050
[6]   INTESTINAL EPITHELIAL DIFFERENTIATION - NEW INSIGHTS FROM CHIMERIC AND TRANSGENIC MICE [J].
GORDON, JI .
JOURNAL OF CELL BIOLOGY, 1989, 108 (04) :1187-1194
[7]   Functional diversity, conservation, and convergence in the evolution of the alpha-, beta-, and gamma-carbonic anhydrase gene families [J].
HewettEmmett, D ;
Tashian, RE .
MOLECULAR PHYLOGENETICS AND EVOLUTION, 1996, 5 (01) :50-77
[8]   HIGH-ACTIVITY CARBONIC-ANHYDRASE ISOENZYME (CA-II) IN HUMAN GALLBLADDER EPITHELIUM [J].
JUVONEN, T ;
PARKKILA, S ;
PARKKILA, AK ;
NIEMELA, O ;
LAJUNEN, LHJ ;
KAIRALUOMA, MI ;
PERAMAKI, P ;
RAJANIEMI, H .
JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY, 1994, 42 (10) :1393-1397
[9]   A HUMAN TRANSMEMBRANE PROTEIN-TYROSINE-PHOSPHATASE, PTP-ZETA, IS EXPRESSED IN BRAIN AND HAS AN N-TERMINAL RECEPTOR DOMAIN HOMOLOGOUS TO CARBONIC-ANHYDRASES [J].
KRUEGER, NX ;
SAITO, H .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (16) :7417-7421
[10]   CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4 [J].
LAEMMLI, UK .
NATURE, 1970, 227 (5259) :680-+