Clunes M T, Lindsay S L, Roussa E, Quinton P M, Bovell D L
School of Biological and Biomedical Sciences, Glasgow Caledonian University, Glasgow G4 0BA, UK.
J Mol Histol. 2004 May;35(4):339-45. doi: 10.1023/b:hijo.0000039837.45595.a6.
The localisation of the vacuolar proton pump (V-H+ -ATPase) and the enzyme carbonic anhydrase II (CAII) was investigated in the human eccrine sweat gland employing standard immunohistochemical techniques after antigen retrieval using microwave heat treatment and high pressure. The high-pressure antigen retrieval unmasked the presence of V-H+ -ATPase in the clear cells of the secretory coil, with a distribution similar to that previously observed for CAII. However, the dark cells were unreactive to both antibodies. In addition, heat and high-pressure antigen retrieval demonstrated the presence of CAII in the apical zone of luminal cells of the reabsorptive duct, a location not previously reported. The localisation of V-H+ -ATPase and CAII in the secretory coil clear cells suggests that the formation of HCO3- and H+ by carbonic anhydrase II and the transport of H+ by V-H+ -ATPase may play an role in sweat fluid secretion. Their presence at the apex of the duct cells indicates involvement in ductal ion reabsorption.
采用微波热处理和高压抗原修复后的标准免疫组织化学技术,研究了人外泌汗腺中液泡质子泵(V-H+-ATP酶)和碳酸酐酶II(CAII)的定位。高压抗原修复显示分泌盘曲部透明细胞中存在V-H+-ATP酶,其分布与先前观察到的CAII相似。然而,暗细胞对两种抗体均无反应。此外,加热和高压抗原修复显示CAII存在于重吸收导管管腔细胞的顶端区域,这是以前未报道过的位置。V-H+-ATP酶和CAII在分泌盘曲部透明细胞中的定位表明,碳酸酐酶II形成HCO3-和H+以及V-H+-ATP酶转运H+可能在汗液分泌中起作用。它们在导管细胞顶端的存在表明参与了导管离子重吸收。