Structure and function of human sweat glands.
| Project/Area Number |
05670738
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Dermatology
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| Research Institution | Sapporo Medical University School of Medicine |
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Principal Investigator |
SAGA Kenji Sapporo Medical University, Dermatology, Assistant Professor, 医学部, 講師 (10153925)
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| Co-Investigator(Kenkyū-buntansha) |
MIURA Shunsuke Sapporo Medical University, Dermatology, Instructor, 医学部, 助手 (50244364)
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| Project Period (FY) |
1993 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1995: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1994: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1993: ¥1,000,000 (Direct Cost: ¥1,000,000)
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| Keywords | eccrine sweat gland / apocrine sweat gland / alkaline phosphatase / anionic sites / glycosaminoglycan / proliferating cell / bromodeoxyuridine / PCNA / 細胞間微小汗管 / 筋上皮細胞 / 酵素消化 / 細胞間微小管 |
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| Research Abstract |
We ultrastructurally localized anionic sites in human eccrine and apocrine sweat glands using poly-L-lysine-gold complex (cationic colloidal gold). In eccrine sweat glands, particles of colloidal gold were restricted to the basolateral membrane of the secretory cells at low pH,whereas the luminal membrane did not react with the gold particles. Chondroitinase ABC digested these anionic sites. This indicates chondroitin sulfate and/or dermatan sulfate constitutes anionic sites in the basal labyrinth of eccrine sweat glands. In apocrine sweat glands, the luminal membrane of the secretory cells showed strong reaction at low pH,whereas the contraluminal membrane did not show any reaction. Neuraminidase completely digested these anionic sites, which indicated anionic charge of apocrine lumen was due to sialic acid.
Alkaline phosphatase (ALP) is a membrane bound enzyme that catalyzes the hydrolysis of inorganic and organic monophosphate esters at alkaline pH.We studied the localization of ALP
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in human sweat glands with light and electron microscopic enzyme cytochemistry. In eccrine sweat glands, ALP was restricted to the cell membranes of intercellular canaliculi. Luminal cell membranes of secretory cells that are in conti nuity with intercellular canaliculi did not show the activity of ALP.These results suggest that ALP may participate in the production of primary sweat at intercellular canaliculi. In apocrine sweat glands, basal cell membranes of secretory cells and myoepithelial cell membranes that were in apposition with each other showed the activity of ALP where no activity was shown in eccrine sweat glands. These differences in the distribution of ALP in myoepithelial cells between eccrine and apocrine sweat glands might be related to the functional differences of these sweat glands.
We studied the proliferating cells in human eccrine and apocrine sweat glands by labeling S-phase cells in vitro with 5-bromo-2'-deoxyuridine (BrdUrd), and by immunostaining proliferation associated proliferating cell nuclear antigen (PCNA) with anti-PCNA monoclonal antibody. The results showed that BrdUrd and anti-PCNA antibody labeled a few secretory cells in eccrine and apocrine sweat glands. On the other hand, neither method labeled myoepithelial cells. Both luminal and peripheral cells of the eccrine and apocrine coiled duct were labeled both with BrdUrd and PCNA.These results suggest that lost secretory cells could be replaced by the proliferation of secretory cells themselves and not by the proliferation of myoepithelial cells or ductal cells. Less
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Report
(4 results)
Research Products
(21 results)
