Aumüller G, Arce E A, Heyns W, Vercaeren I, Dammshäuser I, Seitz J
Insitut für Anatomie und Zellbiologie, Philipps-Universität Marburg, Germany.
Cell Tissue Res. 1995 Apr;280(1):171-81. doi: 10.1007/BF00304522.
Antibodies against 10 different secretory proteins from the accessory sex glands of the male rat were used for immunohistochemical studies of salivary and lacrimal glands from intact and castrated rats, at the light- and electron-microscopic levels. In the parotid gland, secretory acinar cells showed immunoreactivity with antibodies against prostatic binding protein, cystatin-related peptide and acid phosphatase (isoenzyme pI 8.0; 5.6) typical of ventral prostate, and seminal vesicle secretion VI. Western blotting analysis indicated that immunoreactivity against prostatic binding protein was attributable to a subunit, presumably C3. Acid phosphatase pI 5.6 showed a molecular weight of 66 kDa, which is at variance with the prostatic form. Immunoreactivity for secretory transglutaminase, derived from the coagulating gland, was restricted to myoepithelial and stromal cells. In castrated animals, the immunoreactivity of acinar cells was reduced to the background level, whereas stromal transglutaminase immunoreactivity was unaltered. The distribution pattern of immunoreactivity for the proteins mentioned was almost identical in the lacrimal gland. Significant differences were however observed in the immunoreactivity of the inframandibular gland, where serous glandular cells were non-immunoreactive for seminal proteins, with the exception of acid phosphatase isoenzyme pI 8.0. Granules present in the convoluted granular ducts were immunoreactive particularly for acid phosphatase (isoenzyme pI 5.6) but much less for cystatin-related peptide; immunoreactivity was reduced after castration. The straight portion of the inframandibular duct system was immunoreactive for transglutaminase, but no influence of castration was visible. The distribution of immunoreactivity for seminal proteins present in the salivary and lacrimal glands and the pronounced androgen-dependence of their expression point to functional relationships of the respective proteins at both glandular sites.
利用针对雄性大鼠附属性腺10种不同分泌蛋白的抗体，在光镜和电镜水平上对完整和去势大鼠的唾液腺和泪腺进行免疫组织化学研究。在腮腺中，分泌性腺泡细胞对前列腺结合蛋白、胱抑素相关肽和酸性磷酸酶（同工酶pI 8.0；5.6）（典型的前列腺腹侧和精囊分泌物VI）的抗体表现出免疫反应性。蛋白质印迹分析表明，针对前列腺结合蛋白的免疫反应性归因于一个亚基，可能是C3。酸性磷酸酶pI 5.6的分子量为66 kDa，与前列腺形式不同。来自凝固腺的分泌型转谷氨酰胺酶的免疫反应性仅限于肌上皮细胞和基质细胞。在去势动物中，腺泡细胞的免疫反应性降低到背景水平，而基质转谷氨酰胺酶的免疫反应性未改变。上述蛋白质免疫反应性的分布模式在泪腺中几乎相同。然而，在下颌下腺的免疫反应性方面观察到显著差异，其中浆液性腺细胞对精液蛋白无免疫反应性，但酸性磷酸酶同工酶pI 8.0除外。存在于盘曲颗粒管中的颗粒对酸性磷酸酶（同工酶pI 5.6）特别具有免疫反应性，但对胱抑素相关肽的免疫反应性则低得多；去势后免疫反应性降低。下颌下导管系统的直部对转谷氨酰胺酶具有免疫反应性，但未观察到去势的影响。唾液腺和泪腺中精液蛋白免疫反应性的分布及其表达对雄激素的明显依赖性表明了这两个腺部位各自蛋白质之间的功能关系。
