Expression of membrane-bound carbonic anhydrase in developing human lung and kidney

1989 ◽  
Vol 17 (6) ◽  
pp. 1122-1123
Author(s):  
NICK CARTER ◽  
ANTHONY FRYER ◽  
ROBERT HUME ◽  
RICHARD STRANGE ◽  
PER WISTRAND
Keyword(s):  
Carbonic Anhydrase ◽  
Human Lung ◽  
Membrane Bound ◽  
Lung And Kidney

scholarly journals Perfluorobutanoic acid (PFBA): No high-level accumulation in human lung and kidney tissue

2021 ◽  
Vol 237 ◽  
pp. 113830
Author(s):  
Klaus Abraham ◽  
Ahmed H. El-Khatib ◽  
Tanja Schwerdtle ◽  
Bernhard H. Monien
Keyword(s):  
Human Lung ◽  
Kidney Tissue ◽  
High Level ◽  
Lung And Kidney

scholarly journals Location of a membrane-bound carbonic anhydrase isoenzyme (CA IV) in the human male reproductive tract.

1993 ◽  
Vol 41 (5) ◽  
pp. 751-757 ◽  
Author(s):  
S Parkkila ◽  
A K Parkkila ◽  
K Kaunisto ◽  
A Waheed ◽  
W S Sly ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Carbonic Anhydrase ◽  
Reproductive Tract ◽  
Muscle Layer ◽  
Apical Plasma Membrane ◽  
Specific Staining ◽  
Ductus Deferens ◽  
Male Reproductive Tract ◽  
Human Male ◽  
Membrane Bound

We studied the location of a membrane-bound carbonic anhydrase (CA IV) in the human male reproductive tract using a specific antiserum to human CA IV in conjunction with immunoblotting, immunoperoxidase, and immunofluorescence techniques. The microvilli and apical plasma membrane of the epithelial cells and the subepithelial smooth muscle layer of the epididymis, ductus deferens, and ampulla of the ductus deferens showed specific staining for CA IV. The epithelial cells of the prostate and seminal vesicle failed to stain for CA IV, however, whereas the subepithelial smooth muscle layer showed positive staining. No specific staining for CA II was seen in the epithelium of the epididymal duct or the proximal ductus deferens. The presence of CA IV in the epididymis was confirmed by immunoblotting, which revealed 35 KD and 33 KD polypeptides. The results show that the microvilli and the apical plasma membrane of the lining epithelium of the epididymal duct, ductus deferens, and ampulla of the ductus deferens contain the membrane-bound carbonic anhydrase isoenzyme IV. The presence of the enzyme in the epithelium of the epididymis and ductus deferens is probably linked to the acidification of the epididymal fluid that prevents premature sperm activation. Its physiological role in the smooth muscle cells remains to be elucidated.

Localization of carbonic anhydrase in the goat mammary gland during involution and lactogenesis

1998 ◽  
Vol 65 (1) ◽  
pp. 43-54 ◽  
Author(s):  
KATARINA CVEK ◽  
KRISTINA DAHLBORN ◽  
YVONNE RIDDERSTRÅLE
Keyword(s):  
Mammary Gland ◽  
Carbonic Anhydrase ◽  
Time Course ◽  
Ph Regulation ◽  
Late Pregnancy ◽  
Milk Composition ◽  
Tissue Growth ◽  
Systemic Factors ◽  
Membrane Bound ◽  
Alveolar Area

The aim of this study was to determine whether carbonic anhydrase (CA) activity in goat mammary capillaries is regulated mainly by local or systemic mechanisms. One gland was dried before the contralateral gland, and after parturition only one gland was milked. Biopsies were taken from the mammary glands of three goats at 14 d intervals during involution and the start of the following lactation. A histochemical method was used to visualize sites of CA activity. To follow the involution process, milk (liquid) samples were taken from both teats each week and analysed for pH and composition. The time course of CA activity disappearance and reappearance in the capillaries was related to changes in milk composition and alveolar area. A dense network of capillaries showing membrane-bound staining for CA was found surrounding the alveoli in the lactating gland. CA activity gradually decreased in the drying gland, although the other gland was being milked. After 8 weeks involution the dried gland had a significantly lower number of stained capillaries than the milked gland. Almost no stained capillaries were found during late pregnancy, when both glands were dried and the tissue growth maximal. During lactation milk pH was 6·6±0·3 and this increased to 7·0±0·1 in the course of involution. In the last trimester of pregnancy the pH returned to its lower value, while the mammary gland was devoid of stained capillaries. Therefore, the capillary CA could not have been directly involved in the pH regulation of milk. The CA activity reappeared in the capillaries directly after delivery, but only in the milked gland. Clearly the regulation of CA activity is influenced more by local than by systemic factors and is associated with the metabolic activity of milk secretion.

Inhibition of membrane-bound carbonic anhydrase decreases subretinal pH and volume

Macular Edema ◽  
2000 ◽  
pp. 57-67
Author(s):  
Thomas J. Wolfensberger ◽  
Andrey V. Dmitriev ◽  
Victor I. Govardovskii
Keyword(s):  
Carbonic Anhydrase ◽  
Membrane Bound

Plasma membrane-bound carbonic anhydrase activity in the regenerating rat liver

1991 ◽  
Vol 1061 (1) ◽  
pp. 9-14 ◽  
Author(s):  
Jose Juan García Marín ◽  
Arancha Tabernero Urbieta ◽  
Fernando Pérez Barriocanal ◽  
Emilio Rodríguez Barbero ◽  
Nelida Eleno
Keyword(s):  
Plasma Membrane ◽  
Carbonic Anhydrase ◽  
Rat Liver ◽  
Carbonic Anhydrase Activity ◽  
Regenerating Rat Liver ◽  
Membrane Bound

Expression of membrane-associated carbonic anhydrase isoforms IV, IX, XII, and XIV in the rabbit: induction of CA IV and IX during maturation

2005 ◽  
Vol 288 (5) ◽  
pp. R1256-R1263 ◽  
Author(s):  
Jeffrey M. Purkerson ◽  
George J. Schwartz
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Gall Bladder ◽  
Plasma Membranes ◽  
Rabbit Kidney ◽  
Α Subunit ◽  
Anion Transporters ◽  
Ca Ix ◽  
Membrane Bound ◽  
Physiological Demands

Several carbonic anhydrase (CA) isoforms are associated with plasma membranes. It is probable that these enzymes interact with anion transporters to facilitate the movement of HCO3− into or out of the cell. A better knowledge of CA isoform expression in a given tissue would facilitate a systematic examination of any associations with such transporters. We examined the expression of CAs IV, IX, XII, and XIV mRNAs in rabbit tissues, including kidney, heart, lung, skeletal muscle, liver, pancreas, gall bladder, stomach, small intestine, colon, and spleen, using quantitative real-time reverse transcription polymerase chain reaction (RT-PCR). CA IV mRNA was mainly in kidney, heart, lung, colon, and gall bladder. CA IX mRNA was restricted to stomach, gall bladder, duodenum, and early jejunum. CA XII mRNA was found in kidney and colon. CA XIV mRNA was localized to heart, lung, skeletal muscle, and liver. The data indicate that there are different patterns of CA expression in various tissues: CA IX was expressed in the proximal gastrointestinal tract, whereas CA XII and CA IV were more distal. CA IV and CA XII are important kidney isoforms. CA XIV was abundant in metabolically active tissues such as liver, heart, lung, and skeletal muscle. Some significant species differences were noted in the expression of some of these isoforms; for example, CA XIV is not expressed in rabbit kidney, despite being abundant in mouse kidney. Maturational studies showed that the expression of CA IX mRNA and protein increased markedly with weaning (∼3–4 postnatal wk) and was well correlated with the maturational expression of the α-subunit of the gastric H+,K+-ATPase, suggesting that function of CA IX and the gastric H+ pump might be linked in the digestion of adult foodstuffs. The unique pattern of membrane-bound CA isoforms suggests different functional associations with transporters, depending on the physiological demands on the tissue.

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