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ABSTRACT: Cytosolic and secretory carbonic anhydrase isoenzymes (CA-II and CA-VI, respectively) were detected by immunohistolocalization using specific canine CA-II and CA-VI antisera. CA-II and CA-VI were identified in glands associated with the canine lacrimal apparatus, such as lacrimal gland, superficial gland of the third eyelid (third eyelid gland) and tarsal gland. CA-II and CA-VI mRNA signals were also detected by reverse-transcriptase polymerase chain reaction in the same tissues. Some serous acinar cells and duct segments in the lacrimal gland and serous acinar cells in the third eyelid gland were immunopositive for anti-CA-II and CA-VI antisera. In particular, some immunopositive acini to CA-II and CA-VI on the edge of the third eyelid gland are histologically similar to sebaceous gland cells. Sebaceous gland cells in the tarsal and ciliary glands also showed immunopositivity to both CA antisera. CA-II and CA-VI gene transcripts were detected in the same regions. These results suggest that secreted CA-VI may form together with cytosolic CA-II, a high-activity isozyme mostly considered as a bicarbonate producer, in a mutually complementary system for the maintenance of bicarbonate levels to regulate pH in tear fluid and protect the corneal epithelia against injuries. In sebaceous gland cells in the lacrimal apparatus, CA-VI may be related to lipogenesis in an unknown function.
Anantomia Histologia Embryologia 10/2009; 39(1):1-6. · 0.90 Impact Factor
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ABSTRACT: While the mandibular glands usually consist of only mucous acinar cells or a combination of mucous and serous cells in other species of mammals, those of koalas were serous glands. Rabbit mono-specific polyclonal anti-canine CA-I, II, III or VI antiserum showed cross-reactivity against corresponding koala carbonic anhydrase (CA) isozymes. Although immunohistochemical reactions to CA-I, II and VI in ductal cells were moderate to strong in the tested salivary glands, no reaction or only slight reactions were observed against CA-III. In the sublingual glands, moderate immunohistochemical reactions to CA-I, II and VI were also evident in serous acinar cells and serous demilunes. However, no reactions to the tested isozymes were observed in mucous acinar cells in these glands. With the exception of the histological structure of the mandibular glands, histological features and the distributional profile of CA isozymes of the salivary glands in koalas are relatively close to results obtained from horses.
Anantomia Histologia Embryologia 09/2009; 38(6):449-54. · 0.90 Impact Factor
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ABSTRACT: To clarify whether striated duct cells in canine salivary glands synthesize secretory carbonic anhydrase (CA-VI), as is the case with serous acinar cells, the present study utilized laser microdissection to harvest striated duct cells from canine parotid and submandibular glands, and total RNA extracted from these cells was then amplified by reverse transcription-polymerase chain reaction to assess CA-VI gene expression. The results confirmed the local expression of CA-VI mRNA in striated duct cells. This clarified that, in canine salivary glands, CA-VI is synthesized in not only serous acinar cells, but also striated duct cells.
Anantomia Histologia Embryologia 11/2007; 36(5):357-60. · 0.90 Impact Factor
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ABSTRACT: The immunohistolocalization of secretory carbonic anhydrase isoenzymes (CA-VI) in canine salivary glands, parotid, submandibular, sublingual and zygomatic glands, oral and oesophageal mucosa was studied using a specific antiserum against a canine CA-VI. In addition, the gene expression of CA-VI from the same tissue was studied using a real-time reverse-transcriptase polymerase chain reaction. In all salivary glands and oesophageal gland, immunostaining intensely localized CA-VI antiserum throughout the cytoplasm of serous acinar cells, including serous demilune and ductal epithelial cells. In contrast, no immunoreaction localized CA-VI in the mucous acinar cells of the gland. CA-VI gene transcripts were also detected in the same areas. The physiological significance of secretory CA-VI in the oral and oesophageal cavity is thought to play a highly specialized role in the maintenance of bicarbonate level in saliva and to protect mucosa from acid injury. It is shown that the major sites of the CA-VI secretion in dogs were in serous (demilune) secretory cells in all four major salivary glands and oesophageal glands in particular.
Anantomia Histologia Embryologia 03/2007; 36(1):53-7. · 0.90 Impact Factor
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ABSTRACT: The lymph drainage routes from the abdominal cavity in rats were observed at 3 min, 1, 2 and 4 h after India ink was administered intraperitoneally. Four systems of lymph drainage routes from the peritoneal cavity were observed. Three minutes after injection, the drainage route travelled via the intrathoracic lymph vessels located along the internal thoracic artery and returned to the anterior mediastinal lymph nodes. One hour after injection, the drainage route travelled via the lymph vessel located along the left phrenic nerve in addition to the drainage route observed at 3 min. Two and four hours after injection, in addition to the above-mentioned routes, the drainage that had travelled via the thoracic duct continued along the right side of the aorta and was also observed in the lateral lymph vessel located on the vertebra. These findings suggest that lymph or cells absorbed into the peritoneal cavity at first travel towards the anterior mediastinal lymph nodes in the thorax via the ventral lymphatic channels, and then gradually course through the dorsal lymphatic channels. These routes may serve as a route for transporting cancer cells and other cells from the peritoneal cavity.
Anantomia Histologia Embryologia 03/2007; 36(1):78-82. · 0.90 Impact Factor
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ABSTRACT: Concentrations of bovine carbonic anhydrase isozyme VI (CA-IV) in bovine serum, saliva, normal milk, colostrum, submandibular gland, liver, and mammary gland were determined. CA-VI was purified from bovine saliva and an antibody to CA-VI was generated. The concentrations of CA-VI in the saliva (7.8 +/- 7.9 microg/ml), serum (2.1+/- 5.7 ng/ml), milk (7.9 +/- 12.1 ng/ml), submandibular gland (284.7 microg/g protein), liver (921.0 +/- 180.7 ng/g protein) and mammary gland (399.6 +/- 191.2 ng/g protein) were determined by ELISA. No seasonal change in CA-VI levels was observed in normal milk. The concentration of CA-VI in colostrum (day 1 post partum) was 119 ng/ml and decreased rapidly by 1 month following birth. Mammary gland contained much smaller amounts than the submandibular gland. CA-VI mRNA was detected in the liver and mammary gland of cow by RT-PCR. The ELISA used in this study proved to be a precise and sensitive method for determining CA-VI concentrations in saliva, serum, milk and tissue specimens from cows. The ELISA may enable the study of changes in CA-VI associated with hereditary or metabolic disorders of the salivary gland, mammary gland and liver using small samples of saliva, serum or milk.
Veterinary Research Communications 02/2007; 31(1):83-92. · 0.82 Impact Factor
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ABSTRACT: We prepared a map of the cleavage lines for beagle dogs, as a guideline for use of cleavage lines in dermatoplasty. The cleavage lines at the head resembled the orientation of the underlying muscles. Although the cleavage lines in the trunk were perpendicular to the body axis, those in the thoraco-abdominal region were parallel to the body axis. The cleavage lines at the limbs were parallel to the long axis of the limb on the cranial surface, but were perpendicular to the long axis of the limb on the lateral and caudal surfaces. Also, we recorded in detail the cleavage lines in the distal regions of the limbs.
Anantomia Histologia Embryologia 05/2003; 32(2):65-9. · 0.90 Impact Factor
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ABSTRACT: Localizations of carbonic anhydrase isoenzymes (CA I, CA II and CA III) were investigated immunohistochemically in the salivary glands and intestine of mature and suckling pigs. Carbonic anhydrase isoenzymes were not detected in the salivary glands of sucklings, but were present in the adult. Bicarbonate ion in saliva might be important for the digestion of solid foods in mature pigs, but unnecessary for the digestion of milk in sucklings. Expressions of CA I and CA II were detected strongly in the large intestine of the adult and sucklings, and faintly only at duodenum in the small intestine. CA I and CA II isoenzymes in the large intestine may be involved, at least in part, in ion absorption and water metabolism during digestion and absorption of milk in suckling pigs. In addition, CA I and CA II expression in the duodenal villus enterocyte may support the process of bicarbonate absorption in the duodenum.
Journal of Veterinary Medical Science 10/2001; 63(9):967-70. · 0.85 Impact Factor
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ABSTRACT: To purify canine carbonic anhydrase (CA) isoenzymes CA-I and CA-II and to determine concentrations of CA-I and CA-II in erythrocytes of Beagles and dogs native to Japan.
Blood samples from 116 Beagles, including 24 pregnant Beagles, and blood samples from 29 dogs native to Japan.
Canine CA-I and CA-II were purified by use of column chromatography. Concentrations of CA-I and CA-II in erythrocytes of dogs were determined, using an ELISA.
Mean (+/- SD) concentrations of CA-I and CA-II in erythrocytes of Beagles were 3.21+/-0.86 and 1.63+/-0.39 mg/g of Hb, respectively. Mean concentration of CA-I was greater in male Beagles than female Beagles. In contrast, mean concentration of CA-II was greater in female Beagles than male Beagles. Furthermore, concentration of CA-II was greater in pregnant female Beagles than male or nonpregnant female Beagles. Mean concentrations of CA-I and CA-II in erythrocytes of dogs native to Japan were 11.03+/-4.39 and 3.29+/-0.91 mg/g of Hb, respectively. Mean concentration of CA-I was greater in male dogs from Japan than female dogs from Japan.
The ELISA used in this study proved to be precise and sensitive for determining CA-I and CA-II concentrations in dogs. The ELISA may enable study of changes in isoenzymes associated with hereditary or metabolic disorders of blood or other body fluids, using only a small sample. Measurement of the concentrations of CA isoenzymes in dogs may be of diagnostic value.
American Journal of Veterinary Research 05/2000; 61(4):387-92. · 1.27 Impact Factor
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ABSTRACT: The immunohistolocalization of carbonic anhydrase isozymes (CA-I, II, III) in canine salivary glands was studied using antiserum against CA-I, II, III. In parotid glands, immunostaining intensely localized cytosolic CA-II antiserum throughout the cytoplasm of acinar secretory cells and ductal epithelial cells, especially in the striated duct region. CA-III reactivity in the glands was only seen selectively at the intercalated ductal cells. In contrast, no immunoreaction localized CA-I in the gland. In the submandibular and sublingual glands, CA-I, II, and III were all observed in the ductal segments of the glands, whereas serous demilune appeared devoid of all three cytosolic CA isozymes. In contrast, in zygomatic glands (i.e. dorsal buccal glands) all CA isozymes were observed in both serous demilune and ductal segments. In all of the salivary glands examined, no mucous acinar cells were found to be reactive for any CA.
Anantomia Histologia Embryologia 04/2000; 29(1):9-12. · 0.90 Impact Factor
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ABSTRACT: The distribution of bovine carbonic anhydrase isozyme VI (CA-VI), purified from bovine saliva, was studied immunohistochemically using antiserum against bovine CA-VI in bovine parotid glands during fetal and postnatal development. A weak expression of CA-VI in undifferentiated epithelial cells and ductal cells was observed in a 4- to 5-month-old fetus with a 26-cm crown-rump length. The reaction in both acinar and ductal cells subsequently persisted during late gestation and birth. Although anti-CA-VI reactivity was still seen in both regions immediately following birth, the reactivity had almost completely disappeared from most duct segments by 1 month following birth. Changes in the localization and time-dependent expression of the isozyme in parotid glands may reflect changes in the biological function of structurally closely related isozymes.
Cells Tissues Organs 02/2000; 167(1):18-24. · 2.20 Impact Factor
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ABSTRACT: Immunohistochemical localizations of carbonic anhydrase isozymes (CA-I, CA-II and CA-III) in bovine male reproductive tracts were studied. In bulls, no immunoreaction was seen after treatment with antibodies to CA-I, -II and CA-III in the testis. Specific staining for CA-III, however, was evident in peritubular cells in interstitial tissue of the testis, epididymis. CA-II activity could be detected in epithelium of the epididymis, ductus deferentis and ampulla ductus deferentis. Especially, a strong reaction for CA-II was seen in apical in epithelium of the epididymis in the initial and middle segment. CA-I activity was only founded in ductus deferentis and ampulla ductus deferentis. No or a weak reaction for CA-I, CA-II and CA-III were seen in the three accessory reproductive glands. Specific immunostaining for CA-II and CA-I could be observed in the organ, suggesting the bicarbonate in bovine semen to derive primarily from the genital tract and not accessory reproductive organs. CA-III-positive peritubular cells in interstitial tissue were also stained for alpha smooth muscle actin, and were very similar to contractile myofibroblast cells (Wrobel et al., 1979).
Okajimas Folia Anatomica Japonica 01/1998; 74(5):193-8.
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ABSTRACT: Immunohistochemical localization of bovine decorin was examined with its biological analysis in the fetal bovine rumen. By immunohistochemical staining, monoclonal antibody (mAb) 2B6, which recognizes chondroitin 4-sulfate and/or dermatan sulfate (DS), reacted specifically to the lower mesenchymal region in the developing ruminal wall. Biochemical analysis of the extract from the developing rumen revealed that molecule detected immunohistochemically by mAb 2B6 was small DS proteoglycan, bovine decorin. These results support the view that bovine decorin is involved in organization of the fetal bovine ruminal mesenchyme as a collagenous tissue.
Journal of Veterinary Medical Science 03/1997; 59(2):121-3. · 0.85 Impact Factor
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ABSTRACT: The expression and distribution of myoepithelial cells in relation to parotid acinar cells were studied immunohistochemically in bovine fetuses and neonates. Definitive myoepithelial cells first appeared as slender, brown short lines around the perimeters of developing secretion acini at four months of fetal age (in a 26 cm long fetus). At this time, parotid acinar cells possessed no distinct secretory granules in the supranuclear region. The differentiation of myoepithelial cells subsequently progressed during late gestation and birth. In neonates, the myoepithelial cells surrounded the secretory acini and parts of the intercalated ducts.
Okajimas Folia Anatomica Japonica 11/1996; 73(4):205-9.
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Annals of Anatomy - Anatomischer Anzeiger 09/1996; 178(4):369-73. · 1.86 Impact Factor
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ABSTRACT: The membranous bulge lingual to the mandibular molar tooth was examined microscopically in 12 cats and found to contain a small mixed salivary gland. Approximate size of the gland was 1.0-1.5 mm bucco-lingually, 3.0-3.5 mm mesio-distally and 3.0 mm of depth at the largest part. This gland is a tubuloacinar gland with multiple small openings through several short ducts to the surface of the lingual membrane. Mucous acini were predominant with a few serous demilunes.
Journal of veterinary dentistry 06/1996; 13(2):61-4. · 0.31 Impact Factor
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ABSTRACT: To elucidate locations of cytosolic carbonic anhydrase isoenzyme (CA-I, CA-II, and CA-III)-positive epithelial cells in equine male reproductive organs.
Descriptive and immunohistochemical study.
4 clinically normal male horses.
The testis (seminiferous tubules, rete tubules), epididymis (initial, middle, and terminal segments), proximal and distal portions of the ductus deferens, ampulla ductus deferentis, seminal vesicle, prostate, and bulbourethral gland were excised from euthanatized horses after administration of an overdose of pentobarbital. The tissue specimens were quickly placed in fixative solution, dehydrated in ethanol, and embedded; then thin sections were cut. For immunohistochemical staining, antibodies against purified equine CA-I, CA-II, and CA-III were raised in rabbits. After examination of the specificity of each antiserum, the monospecific antisera against carbonic anhydrase isoenzymes were used to localize the isoenzymes.
Specific staining for CA-III was found in the Sertoli and basal cells of the ductus deferens. Most of the testicular and epididymal tissue, as well as ductus deferens, were virtually negative for the enzymes when stained with the antibody to CA-I and CA-II. In the initial segment of the epididymis, a few principal cells had intense cytoplasmic staining with anti-CA-II. In the male accessory glands, CA-I, CA-II, and CA-III were detected in the epithelial cells of the seminal vesicle, prostate, and bulbourethral gland.
In the equine male reproductive tract, the bicarbonate in semen originates mainly from accessory reproductive glands. All 3 isoenzymes may have central roles in the regulation of bicarbonate concentration in seminal plasm and, accordingly, regulate seminal plasma pH. Distribution of CA-III in Sertoli and basal cells of the ductus deferens suggests other specialized physiologic roles.
American Journal of Veterinary Research 05/1996; 57(4):439-43. · 1.27 Impact Factor
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ABSTRACT: The present paper demonstrates the immunohistochemical distribution of proteoglycan (PG) molecules carrying chondroitin sulfate (CS) chains with 6-sulfated hexosamine residues, or CS and/or dermatan sulfate (DS) chains with 4-sulfated residues in the developing bovine ruminal papillae (RP) using monoclonal antibodies (mAbs) 3B3, 2B6, and MO225. These PGs carrying chondroitin 6-sulfate that were detected by mAb 3B3, and the glucuronic acid 2-sulfate-N-acetyl-galactosamine 6-sulfate unit that was detected by the mAb MO225 were distributed in the mesenchyme and epithelial basement membrane in the rumen, and were thus correlated to the outgrowth of the RP. The PG carrying DS was detected by the mAb 2B6 and was distributed in the lower region of the mesenchyme and intermuscular connective tissue during the development of the RP. These findings suggest that PGs carrying CS chains with 6-sulfation are involved in the outgrowth of the RP, and that PGs carrying DS are involved in organization in the mesenchyme.
Acta Anatomica 02/1996; 156(4):283-8.
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ABSTRACT: The present paper demonstrates the immunohistochemical distribution of proteoglycan (PG) molecules carrying chondroitin sulfate (CS) chains with 6-sulfated hexosamine residues, or CS and/or dermatan sulfate (DS) chains with 4-sulfated residues in the developing bovine ruminal papillae (RP) using monoclonal antibodies (mAbs) 3B3, 2B6, and MO225. These PGs carrying chondroitin 6-sulfate that were detected by mAb 3B3, and the glucuronic acid 2-sulfate-N-acetyl-galactosamine 6-sulfate unit that was detected by the mAb MO225 were distributed in the mesenchyme and epithelial basement membrane in the rumen, and were thus correlated to the outgrowth of the RP. The PG carrying DS was detected by the mAb 2B6 and was distributed in the lower region of the mesenchyme and intermuscular connective tissue during the development of the RP. These findings suggest that PGs carrying CS chains with 6-sulfation are involved in the outgrowth of the RP, and that PGs carrying DS are involved in organization in the mesenchyme.
Cells Tissues Organs 02/1996; 156(4):283-288. · 2.20 Impact Factor
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ABSTRACT: Insulin has a plethora of metabolic effects but its action on carbonic anhydrase-III (CA-III), a key enzyme in acid-base regulation, has been little studied. The present studies examined the effects of streptozotocin induced diabetes on the concentrations of CA-III. The concentration of CA-III in the liver, muscles and serum of rats with experimental diabetes mellitus was measured by the method of enzyme-immunoassay. Streptozotocin-induced diabetes mellitus resulted in a reduction in concentration of CA-III in the liver and serum, but not in skeletal muscles, of adult male rats. A 98% reduction in hepatic CA-III content relative to control values was observed. The reduction in CA-III content in the liver was restored to control value by administration of insulin. The CA-III content in serum of diabetic rats declined to approx. 25% of control values, but the reduction was unaffected by administration of insulin. The concentration of CA-III in the liver and serum of diabetic rats was not influenced by administration of methyltestosterone. Although the content of CA-III in m. rectus femoris, m. tibialis craniaris and m. soleus differed, no significant difference of CA-III content was found between diabetes mellitus and control rats. The effect of chronic diabetes mellitus on CA-III content was obviously different between liver and muscle, suggesting that the regulation of CA-III biosynthesis differs between these two tissues. These results suggest that biosynthesis of CA-III in hepatocytes of rats is influenced by irregular patterns of GH secretion brought about by diabetes mellitus.
The International Journal of Biochemistry & Cell Biology 05/1995; 27(4):359-64. · 4.63 Impact Factor
