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Irisin was first identified in muscle cells. We detected irisin immunoreactivity in various organs of the crested porcupine (Hystrix cristata). In the epidermis, irisin immunoreactivity was localized mainly in stratum basale, stratum spinosum and stratum granulosum layers; immunoreactivity was not observed in the stratum corneum. In the dermis, irisin was found in the external and internal root sheath, cortex and medulla of hair follicles, and in sebaceous glands. Irisin immunoreactivity was found in the neural retina and skeletal muscle fibers associated with the eye. The pineal and thyroid glands also exhibited irisin immunoreactivity.

Irisin was first identified in skeletal muscle cells. It is an exercise protein that is secreted into the circulation; it causes conversion of white adipose tissue to brown adipose tissue. We investigated irisin immunoreactivity in mole rat (Spalax leucodon) tissues. We examined cerebellum, pituitary, heart, liver, pancreas, spleen, uterus, kidney and striated muscle in female adult mole rats. Tissues were processed, embedded in paraffin, sectioned at 5 μm and stained immunohistochemically for irisin. Irisin immunostaining was detected in the cytoplasm of stained cells; the cytoplasm of Purkinje cells was unstained. We found that irisin may be synthesized in many tissues. The function of locally synthesized irisin currently is unknown.

Irisin is mainly secreted by heart and skeletal muscle cells. It is an exercise-induced protein that converts white adipose tissue to brown. Increased irisin expression was lead to weight loss and improved glucose tolerance. We investigated irisin immunoreactivity in various tissues of the dwarf hamsters (Phodopus roborovskii). Tissues were processed, embedded in paraffin, sectioned at 5 μm and stained immunohistochemically for irisin. In the retina, irisin was found almost all layers, except outer nuclear layer. Also, irisin immunoreactivity was observed in the skin, cornea, striated muscle, parotid gland, tongue, oesophagus, stomach and small intestine. The findings from this study support the notion that skeletal muscle is not the primary source of irisin.

ABSTRACT:The localization of calbindin-D28k was examined in rat kidney at different stages of development. Calbindin was found specifically in the distal convoluted tubules (DCT). In the 10 day old rat kidney many cells apparently belonging to the collecting tubules were positive. In the neonatal nephrons there was also localization of calbindin-D28k to the limb of Henle, suggesting a difference in the regulation of intracellular calcium during maturation. Proximal tubule, renal corpuscle and macula densa gave no specific localization of calbindin-D28k.

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Irisin, a novel peptide, was initially been shown to be expressed explicitly in the muscle tissues. We studied the presence of irisin immunoreactivity in porcupine adrenal glands and kidneys. Immunocytochemistry showed that irisin was localised both in the adrenal cortex and adrenal medulla. In organs, irisin immunoreactivity was found in the tubular and collecting system of the nephron. The functional role of irisin in the adrenal gland and kidney has not been precisely yet. However, irisin might have a paracrine and autocrine function as do other locally produced peptides.

In the present study, the existence of serotonin immunoreactivity was investigated in the adrenal gland and kidney of porcupine, Hystrix cristata, using immunohistochemical techniques as a pioneer attempt. Serotonin immunoreactivity was detected in adrenal medullary cells, distal tubules and collecting duct cells in kidney.