scholarly journals Coexistence of renin and cathepsin B in secretory granules of granular duct cells in male mouse submandibular gland.

1993 ◽  
Vol 41 (3) ◽  
pp. 433-438 ◽  
Author(s):  
K Sano ◽  
S Waguri ◽  
N Sato ◽  
E Kominami ◽  
Y Uchiyama
Keyword(s):  
Submandibular Gland ◽  
Golgi Complex ◽  
Cathepsin B ◽  
Cysteine Proteinase ◽  
Secretory Granules ◽  
Interstitial Cells ◽  
Double Immunostaining ◽  
Duct Cells ◽  
Cathepsin H ◽  
Rat Pituitary

Cathepsin B, a representative lysosomal cysteine proteinase, has been demonstrated to coexist with renin in secretary granules of rat pituitary LH/FSH cells and renal juxtaglomerular cells. We investigated immunocytochemically the localization of cathepsins B, H, and L in the submandibular gland of male mice, in which active renin is also produced. By light microscopy, granular immunodeposits for cathepsin B were detected in epithelial cells of the gland, particularly in granular duct cells and interstitial cells. Immunoreactivity for cathepsins H and L was mainly found in interstitial cells, although that for cathepsin H was weakly seen in acinar cells. By electron microscopy, immunogold particles indicating cathepsin B intensely labeled small granules near the Golgi complex of granular duct cells and weakly labeled large secretory granules, whereas those showing renin labeled both granules. Double immunostaining co-localized immunogold particles showing renin and cathepsin B in small perinuclear granules near the Golgi complex. Some immunopositive granules seemed to be closely associated with the Golgi elements. These results indicate that the co-localization of renin and cathepsin B is also seen in secretory granules of granular duct cells in the mouse submandibular gland, as seen in rat juxtaglomerular and LH/FSH cells. This suggests that cathepsin B is one of the possible candidates for the renin-processing enzyme.

scholarly journals Ultrastructural immunolocalization of kallikrein in apical granules of striated duct cells of cat submandibular gland.

1983 ◽  
Vol 31 (2) ◽  
pp. 345-347 ◽  
Author(s):  
M Schachter ◽  
G D Wheeler ◽  
R W Matthews ◽  
M W Peret ◽  
C Moriwaki
Keyword(s):  
Serine Protease ◽  
Submandibular Gland ◽  
Direct Evidence ◽  
Immune Reaction ◽  
Secretory Granules ◽  
Ultrastructural Level ◽  
Circumstantial Evidence ◽  
Duct Cells

Recent studies on the localization of the serine protease salivary kallikrein have led to the conclusion that it has a ductal localization and to the possibility that it is located there in small "secretory" granules. Until now, the latter inference has been based entirely on circumstantial evidence. In the present study, however, direct evidence from immunolocalization studies at the ultrastructural level establishes the localization of this enzyme in the apical duct granules in the cat submandibular gland. These granules stained only with immune sera to cat submandibular gland kallikrein and were the only subcellular structures that did so. They showed the "studded" appearance characteristic of the electron-dense aggregates of peroxidase-antiperoxidase seen in this type of immune reaction.

scholarly journals Immunocytochemical localization of cathepsins B, H, and their endogenous inhibitor, cystatin beta, in islet endocrine cells of rat pancreas.

1988 ◽  
Vol 36 (7) ◽  
pp. 783-791 ◽  
Author(s):  
M Watanabe ◽  
T Watanabe ◽  
Y Ishii ◽  
H Matsuba ◽  
S Kimura ◽  
...  
Keyword(s):  
Endocrine Cells ◽  
Islet Cells ◽  
Secretory Granules ◽  
Double Immunostaining ◽  
Thin Sections ◽  
Cathepsin H ◽  
Immunocytochemical Techniques ◽  
The Difference ◽  
Immunocytochemical Reaction ◽  
Strong Immunoreactivity

To determine the characteristics of lysosomes in rat islet endocrine cells, we examined the precise localization of cathepsins B, H, and L and their specific inhibitors, cystatins alpha and beta, using immunocytochemical techniques. By use of serial semi-thin sections, we detected immunoreactivity for cathepsin B in insulin-, glucagon-, somatostatin-, and pancreatic polypeptide-positive (PP) cells. Strong immunoreactivity for cathepsin H was seen in A-cells and weak immunoreactivity in PP cells, but none in others. Immunodeposits for cystatin beta were demonstrated in B-cells. Brief dipping of thin sections in 1% sodium methoxide before the following immunocytochemical reaction enhanced specific deposits of immunogold particles on the target organelles. Use of a double-immunostaining technique showed co-localization of insulin with cystatin beta in many secretory granules. This suggests that cystatin beta may regulate converting enzymes participating in the maturation process of insulin. By use of an immunogold technique, heterogeneous localization of cathepsins B and H in lysosomes was also found among islet cells at the light microscopic level. This may be due to the difference in peptides degraded in lysosomes among the cells.

scholarly journals Demonstration of cathepsins B, H and L in xenografts of normal and Duchenne-muscular-dystrophy muscles transplanted into nude mice

1992 ◽  
Vol 288 (2) ◽  
pp. 643-648 ◽  
Author(s):  
A Takeda ◽  
T Jimi ◽  
Y Wakayama ◽  
N Misugi ◽  
S Miyake ◽  
...  
Keyword(s):  
Duchenne Muscular Dystrophy ◽  
Muscular Dystrophy ◽  
Nude Mice ◽  
Cathepsin B ◽  
Cysteine Proteinase ◽  
Normal Subjects ◽  
Muscle Fibres ◽  
Cysteine Proteinase Inhibitor ◽  
Normal Muscle ◽  
Cathepsin H

The activities and contents of the lysosomal cysteine proteinases cathepsins B, H and L were examined in xenografts of biopsied muscles transplanted from age-matched normal subjects and Duchenne-muscular-dystrophy (DMD) patients into nude mice. The activity of cathepsin B increased 9-fold and that of B-plus-L increased 24-fold in the first week after transplantation in normal muscle xenografts. By the third week, the activity of cathepsin B increased a total of 20-fold and B-plus-L increased to 36-fold the original level. The activity levels of cathepsin B, B-plus-L, H and D, and acid phosphatase in normal and DMD xenografts were not significantly different when compared 2 weeks after transplantation. However, the protein content of cathepsin B in DMD muscle xenografts was more than 3-fold that of normal xenografts at 2 weeks. The profile of cathepsin H activity in normal muscle xenografts was different than those of cathepsins B and B-plus-L. In the first week, the cathepsin H diminished sharply to about one-third of the biopsied muscle level and then, by 3 weeks after transplantation, it had increased slightly to about half the original level. The amount of endogenous cysteine-proteinase inhibitor changed in parallel with the activity of cathepsins B and B-plus-L. Cathepsins B and H, but not cathepsin L, were found immunohistochemically in regenerating muscle fibres of normal and DMD xenografts 2 weeks after transplantation. Staining of cathepsin B in DMD xenografts was slightly stronger than that in normal subjects. There was no immunostaining in degenerating or necrotic muscle fibres 2 weeks after transplantation. Western-blot analysis revealed that the cathepsin B band at 29 kDa was increased in normal xenografts 2 and 3 weeks after transplantation. Also, 2 weeks after transplantation the staining intensity of this band was slightly stronger in DMD xenografts than in normal xenografts. These results suggest that cathepsin B participates in the regeneration of transplanted muscle, both normal and DMD, and in the DMD muscle fibre-wasting processes, during regeneration.

scholarly journals A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and −161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide catalysed by cathepsin B and of l-arginine 2-naphthylamide catalysed by cathepsin H.

1985 ◽  
Vol 227 (2) ◽  
pp. 521-528 ◽  
Author(s):  
F Willenbrock ◽  
K Brocklehurst
Keyword(s):  
Catalytic Activity ◽  
Cathepsin B ◽  
Cysteine Proteinase ◽  
Ion Pairs ◽  
Preceding Paper ◽  
Structural Features ◽  
Catalytic Site ◽  
Cysteine Proteinases ◽  
Cathepsin H ◽  
Ph Range

The pH-dependences of kcat, Km and kcat./Km for the hydrolysis at 25 degrees C at I 0.1 of L-arginine 2-naphthylamide catalysed by cathepsin H from bovine spleen were determined in the pH range approx. 4-8. The pH-dependences of these kinetic parameters were determined also for the hydrolysis at 25 degrees C at I 0.1 of N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide catalysed by cathepsin B (EC 3.4.22.1) from bovine spleen in the pH range 7-8, which extends the studies in acidic media reported by Willenbrock & Brocklehurst [(1984) Biochem. J. 222, 805-814]. These results are discussed and related to those from the reactivity-probe kinetics reported in the preceding paper [Willenbrock & Brocklehurst (1985) Biochem. J. 227, 511-519] and to known structural features present in rat liver cathepsins B and H and in papain (EC 3.4.22.2) and actinidin (EC 3.4.22.14). Consideration of the kinetic data leads to the suggestion that in the cysteine proteinases rearrangement of intimate S-/ImH+ ion-pairs in catalytic sites is brought about by a combination of field effects in the immediate vicinity of the ion-pair and consequences of protonic dissociation of a group with pKa 5-6 remote from the catalytic site. The contributions of the two types of effect seem to differ from enzyme to enzyme. Of the four cysteine proteinases considered, only cathepsin B exerts an absolute requirement for the proton-deficient form of a group with pKa 5-6 for catalytic activity. Protonic dissociation with pKa 5-6 enhances catalytic activity in cathepsin H and in actinidin and appears to have little or no effect in papain. Only cathepsin B lacks a polar or negatively charged side chain in the residue analogous to Asp-158 in papain, and this is suggested to account for its total dependence on a protonic dissociation remote from the catalytic site.

scholarly journals Expression of transforming growth factor beta 1 in the submandibular gland of the rat.

1991 ◽  
Vol 39 (12) ◽  
pp. 1707-1711 ◽  
Author(s):  
O Amano ◽  
T Tsuji ◽  
T Nakamura ◽  
S Iseki
Keyword(s):  
Growth Factor ◽  
Submandibular Gland ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Secretory Granules ◽  
Female Rats ◽  
Tgf Beta ◽  
Duct Cells ◽  
Growth Factor Beta ◽  
Rat Submandibular Gland

We employed immunocytochemical and in situ hybridization techniques to study the expression of transforming growth factor beta 1 (TGF-beta 1) in rat submandibular gland. Immunoreactivity for TGF-beta 1 was observed in the cells of granular convoluted tubules (GCTs), striated ducts, and excretory ducts, whereas it was absent in the intercalated ducts and secretory acini in both male and female rats. Immunoelectron microscopy revealed the ultrastructural localization of TGF-beta 1 in the secretory granules of GCT cells. On the other hand, signals for rat TGF-beta 1 mRNA were abundant in the GCT and striated duct cells but were lacking in the excretory duct cells. These results provided evidence for the production of TGF-beta 1 in the GCTs and striated ducts of rat submandibular gland.

scholarly journals Immunocytochemical localization of cathepsin B in rat anterior pituitary endocrine cells, with special reference to its co-localization with renin and prorenin in gonadotrophs.

1991 ◽  
Vol 39 (9) ◽  
pp. 1199-1205 ◽  
Author(s):  
Y Uchiyama ◽  
M Nakajima ◽  
T Watanabe ◽  
S Waguri ◽  
N Sato ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Luteinizing Hormone ◽  
Light Microscopy ◽  
Cathepsin B ◽  
Anterior Pituitary ◽  
Endocrine Cells ◽  
Secretory Granules ◽  
Juxtaglomerular Cells ◽  
Immunocytochemical Localization ◽  
Double Immunostaining

We examined by immunocytochemistry the localization of cathepsin B in endocrine cells of rat anterior pituitary lobe, using a monospecific antibody to cathepsin B. By light microscopy, granular immunodeposits for cathepsin B were detected in most endocrine cells of anterior pituitary lobe. Cells immunoreactive for luteinizing hormone (LH) were diffusely immunostained by anti-cathepsin B. By electron microscopy, immunogold particles for cathepsin B were localized in lysosomes of thyrotrophs, somatotrophs, and mammotrophs. In mammotrophs, immunogold particles for cathepsin B were also detected in crinophagic bodies. Double immunostaining co-localized immunogold particles for LH and cathepsin B in secretory granules of gonadotrophs. Immunocytochemistry was also applied to demonstrate localization of renin and prorenin in LH-producing gonadotrophs; immunogold particles for renin were co-localized with those for LH, cathepsin B, or prorenin in their secretory granules. Immunogold particles for prorenin were also co-localized with those for LH or cathepsin B in secretory granules, but prorenin-positive granules appeared less frequently than renin-positive granules. These results suggest that cathepsin B not only plays a role in the protein degradation in lysosomes of anterior pituitary endocrine cells but also participates in the activation of renin in gonadotrophs, as has been demonstrated in secretory granules of juxtaglomerular cells.

scholarly journals THE FINE STRUCTURE OF VON EBNER'S GLAND OF THE RAT

1970 ◽  
Vol 44 (2) ◽  
pp. 340-353 ◽  
Author(s):  
Arthur R. Hand
Keyword(s):  
Fine Structure ◽  
Cell Membrane ◽  
Golgi Complex ◽  
Secretory Granules ◽  
Myoepithelial Cells ◽  
Duct Cells ◽  
Golgi Region ◽  
Granule Membrane ◽  
Cytological Features ◽  
Basal Portion

The fine structure of von Ebner's gland was studied in untreated rats and rats stimulated to secrete by fasting-refeeding or injection of pilocarpine. Cytological features were similar to those reported for pancreas and parotid gland. Abundant granular endoplasmic reticulum filled the basal portion of the cell, a well-developed Golgi complex was located in the vicinity of the nucleus, and the apical portion of the cell was filled with dense secretory granules. Dense heterogeneous bodies resembling lysosomes were closely associated with the Golgi complex. Coated vesicles were seen in the Golgi region and also in continuity with the cell membrane. Granule discharge occurred by fusion of the granule membrane with the cell membrane at the secretory surface. Successive fusion of adjacent granules to the previously fused granule formed a connected string of granules in the apical cytoplasm. Myoepithelial cells were present within the basement membrane, and nerve processes were seen adjacent to acinar and myoepithelial cells. Duct cells resembled the intercalated duct cells of the major salivary glands.

Pituitary Follicular Cells: Their Origin, Possible Function and Fate

1974 ◽  
Vol 32 ◽  
pp. 34-35
Author(s):  
E. Horvath ◽  
K. Kovacs ◽  
G. Penz ◽  
C. Ezrin
Keyword(s):  
Fine Structure ◽  
Secretory Granules ◽  
Follicular Cells ◽  
Human Pituitary ◽  
Rat Pituitary ◽  
Pituitary Glands ◽  
Junctional Complexes

Follicular structures, in the rat pituitary, composed of cells joined by junctional complexes and possessing few organelles and few, if any, secretory granules, were first described by Farquhar in 1957. Cells of the same description have since been observed in several species including man. The importance of these cells, however, remains obscure. While studying human pituitary glands, we have observed wide variations in the fine structure of follicular cells which may lead to a better understanding of their morphogenesis and significance.

Ultrastructural Aspects of Golgi Complex Function in Parathyroid Cells of Winter Frogs

1973 ◽  
Vol 31 ◽  
pp. 680-681
Author(s):  
William J. Dougherty
Keyword(s):  
Golgi Complex ◽  
Secretory Granules ◽  
Complex Function ◽  
Secretory Activity ◽  
Secretory Proteins ◽  
Perivascular Spaces ◽  
Pituitary Cells ◽  
Electron Microscopic ◽  
Ca Ions ◽  
Regulation Of Secretion

The regulation of secretion in exocrine and endocrine cells has long been of interest. Electron microscopic and other studies have demonstrated that secretory proteins synthesized on ribosomes are transported by the rough ER to the Golgi complex where they are concentrated into secretory granules. During active secretion, secretory granules fuse with the cell membrane, liberating and discharging their contents into the perivascular spaces. When secretory activity is suppressed in anterior pituitary cells, undischarged secretory granules may be degraded by lysosomes. In the parathyroid gland, evidence indicates that the level of blood Ca ions regulates both the production and release of parathormone. Thus, when serum Ca is low, synthesis and release of parathormone are both stimulated; when serum Ca is elevated, these processes are inhibited.

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