Impact of Ultraviolet C Radiation on Male Fertility in Rats: Suppression of Autophagy, Stimulation of Gonadotropin-Inhibiting Hormone, and Alteration of miRNAs.

While ultraviolet C (UVC) radiation has beneficial applications, it can also pose risks to living organisms. Nevertheless, a detailed assessment of UVC radiation's effects on mammalian male reproductive physiology, including the underlying mechanisms and potential protective strategies, has not yet been accomplished. This study aimed to examine the critical roles of oxidative stress, autophagy, reproductive hormonal axis, and microRNAs in UVC-induced reproductive challenges in male rats.

Role of Macroautophagy in Mammalian Male Reproductive Physiology.

Physiologically, autophagy is an evolutionarily conserved and self-degradative process in cells. Autophagy carries out normal physiological roles throughout mammalian life. Accumulating evidence shows autophagy as a mechanism for cellular growth, development, differentiation, survival, and homeostasis.

Irisin/FNDC5: A participant in camel metabolism.

The quantification, localization, production, function, and regulation of irisin/FNDC5 in camel species have not been previously studied. The objective of this study was to detect the irisin content in Arabian camel blood and tissues and study the gene expression of FNDC5 and PGC-1α in camel skeletal muscles and white adipose tissue depots under basal conditions. To monitor if exercise influences blood and tissue irisin protein levels as well as FNDC5 and PGC-1α gene expression levels, we analyzed irisin concentrations in the serum, skeletal muscles (soleus and gastrocnemius), and white adipose tissues (hump, subcutaneous, visceral, epididymal, and perirenal) in both control (n = 6) and exercised group (n = 6) using ELISA and determined the cellular localization of irisin/FNDC5 and the mRNA levels of FNDC5 and PGC-1α in skeletal muscles and adipose tissues via immunohistochemistry and real-time PCR, respectively.

Angiotensin II up-regulates monocarboxylate transporters expression in the rat adrenal gland.

Angiotensin II (Ang II) is a major regulator of aldosterone secretion in the adrenal zona glomerulosa because it up-regulates the expression of a large number of genes involved in aldosterone biosynthesis. The transport of acetate across adrenocortical cells is a crucial step in the de novo synthesis of cholesterol, the steroid precursor of aldosterone. However, whether Ang II can affect this transport remains unknown.

Regional and cellular distribution of monocarboxylate transporters 13 and 14 in the cattle gastrointestinal tract.

Understanding of the basic function of orphan transporters can only be achieved by examining their cellular location. This study is the first to describe the precise cellular localization of the orphan monocarboxylate transporters (MCT13) and (MCT14) in the physiologically distinct regions of the gastrointestinal tract of mammals. The present study demonstrated conclusively the regional distribution and relative expression levels of MCT13 and MCT14 on both mRNA and protein levels in the cattle gastrointestinal tract.

The monocarboxylate transporters exist in the cattle endocrine pancreas.

Extensive studies are published concerning the distribution of monocarboxylate transporters (MCTs) in various animal issues including ruminants; nonetheless, nothing is known about their cellular expression and localization in the ruminant pancreas. The present study was carried out to examine the expression and cellular localization of all the fourteen MCT isoforms in cattle pancreas. RT-PCR verified the existence of mRNA transcripts for eight MCT isoforms, namely, MCT1, MCT2, MCT3, MCT4, MCT5, MCT8, MCT13, and MCT14 in cattle pancreas.

Expression and cellular localization of monocarboxylate transporters (MCT2, MCT7, and MCT8) along the cattle gastrointestinal tract.

Fourteen members of the monocarboxylate transporter (MCT, SLC16) family have been identified, each having a different tissue distribution and substrate specificity. The expression of monocarboxylate transporters MCT1 and MCT4 have been studied in the gastrointestinal tract of ruminants; however, details of the expression of other MCT isoforms in the various parts of ruminant gastrointestinal tract are lacking. Reverse transcription with the polymerase chain reaction was used to study the regional distribution of MCT2, MCT3, and MCT5-MCT14 in the cattle gastrointestinal tract and verified the existence of MCT mRNA transcripts for MCT2, MCT3, MCT4, MCT7, MCT8, MCT9, MCT10, MCT13, and MCT14 in the ruminal and abomasal epithelia, mRNA transcripts for MCT2, MCT3, MCT4, MCT7, MCT8, MCT10, MCT13, and MCT14 in the jejunum, and mRNA transcripts for MCT2, MCT3, MCT4, MCT7, MCT8, MCT13, and MCT14 in the caecum of cattle.

Monocarboxylate transporter genes in the mammary gland of lactating cows.

This study is the first to examine the expression of the 14 monocarboxylate transporter genes (MCT1-MCT14) in the mammary gland of mammals. RT-PCR, Western blot, immunohistochemistry, and immunofluorescence confocal laser microscopy were applied in a comprehensive approach to assess the expression and cellular localization of MCTs in the mammary gland of lactating cattle. RT-PCR revealed the existence of nine MCT isoforms, namely MCT1, MCT2, MCT3, MCT4, MCT5, MCT8, MCT10, MCT13, and MCT14 in cow mammary gland.

Effect of pectin feeding on monocarboxylate transporters in rat adrenal gland.

We have recently proved the expression and localization of seven monocarboxylate transporters (MCT1, MCT2, MCT3, MCT4, MCT5, MCT7, and MCT8) in the rat adrenal gland. So far, there are no data reporting possible regulation of any MCT isoform in the adrenal gland. Pectin is a soluble dietary fiber that is known to exert a hypocholesterolemic effect and increases the short chain fatty acids production in the large intestine.

Dietary pectin up-regulates monocaboxylate transporter 1 in the rat gastrointestinal tract.

This work was undertaken to study the effect of pectin feeding on the expression level, cellular localization and functional activity of monocarboxylate transporter 1 (MCT1) in the gastrointestinal tract of rats. The results indicated that MCT1 protein level was significantly increased along the entire length of the gastrointestinal tract of pectin-fed rats in comparison with control animals. Immunohistochemical analysis revealed an increase in MCT1 in the stratified squamous epithelia of the forestomach as well as in the basolateral membranes of the cells lining the gastric pit of the glandular stomach of pectin-fed rats when compared with control animals.

Presence of ten isoforms of monocarboxylate transporter (MCT) family in the bovine adrenal gland.

This study provides novel information regarding the existence and precise cellular localization of various monocarboxylate transporters (MCTs) in the mammalian adrenal gland. RT-PCR results revealed that 10 MCT isoforms, namely MCT1, MCT2, MCT3, MCT4, MCT5, MCT8, MCT9, MCT10, MCT13, and MCT14 are expressed in the bovine adrenal gland. MCTs (MCT1-MCT8) proteins were examined by Western blot analysis in the bovine adrenal gland.

Expression of monocarboxylate transporter 1 (MCT1) in the dog intestine.

In this study, the expression and distribution of monocarboxyolate transporter 1 (MCT1) along the intestines (duodenum, jejunum, ileum, cecum, colon and rectum) of dogs were investigated at both the mRNA and protein levels. The expression of MCT1 protein and its distribution were confirmed by Western blotting and immunohistochemical staining using the antibody for MCT1. We identified mRNA coding for MCT1 and a 43-kDa band of MCT1 protein in all regions from the duodenum to the rectum.

Expression of monocarboxylate transporter 1 in oral and ocular canine melanocytic tumors.

Solid tumors are composed of a heterogeneous population of cells surviving in various concentrations of oxygen. In a hypoxic environment, tumor cells generally up-regulate glycolysis and, therefore, generate more lactate that must be expelled from the cell through proton transporters to prevent intracellular acidosis. Monocarboxylate transporter 1 (MCT1) is a major proton transporter in mammalian cells that transports monocarboxylates, such as lactate and pyruvate, together with a proton across the plasma membrane.

Expression, cellular localization, and functional role of monocarboxylate transporter 4 (MCT4) in the gastrointestinal tract of ruminants.

This is the first study to determine the precise cellular localization of monocarboxylate transporter 4 (MCT4), along with its co-existence with its chaperone, CD147 in the ruminant gastrointestinal tract. Quantitative Western blot analysis demonstrated that the abundance of MCT4 protein was in the order of forestomach > large intestine > abomasum >or= small intestine. Immunohistochemistry and immunofluorescence confocal laser microscopy showed that MCT4 in the forestomach was confined to the cell membranes of strata corneum and granulosum, while diffuse cytoplasmic staining for MCT4 was visualized in strata spinosum and basale.

Monocarboxylate transporter 1 (MCT1) plays a direct role in short-chain fatty acids absorption in caprine rumen.

Despite the importance of short-chain fatty acids (SCFA) in maintaining the ruminant physiology, the mechanism of SCFA absorption is still not fully studied. The goal of this study was to elucidate the possible involvement of monocarboxylate transporter 1 (MCT1) in the mechanism of SCFA transport in the caprine rumen, and to delineate the precise cellular localization and the level of MCT1 protein along the entire caprine gastrointestinal tract. RT-PCR revealed the presence of mRNA encoding for MCT1 in all regions of the caprine gastrointestinal tract.

Monocarboxylate transporter 1 (MCT1) mediates transport of short-chain fatty acids in bovine caecum.

The present study was undertaken to investigate the functional role of monocarboxylate transporter 1 (MCT1) in the ruminant large intestine. Messenger RNA encoding for MCT1 was verified by reverse transcriptase-polymerase chain reaction in caecum, proximal colon and distal colon of adult cattle. Both immunohistochemistry and confocal laser microscopy verified that the MCT1 protein was abundant in the surface epithelium of the large intestine, and the amount decreased from the opening of the crypt to its base.

Monocarboxylate transporter 1 gene expression in the ovine gastrointestinal tract.

In this study, we investigated the tissue distribution and expression of monocarboxylate transporter 1 (MCT1) along the gastrointestinal tract of sheep. Western blot analysis suggested the presence of MCT1 as a 43-kDa protein in immunoblots of membranes from the various tissues examined. The results of Western blotting were further confirmed by immunohistochemical studies, which revealed intense immunoreactivity for the MCT1 protein in the forestomach (rumen, reticulum and omasum) and large intestine (caecum, proximal and distal colon).

Monocarboxylate transporter 1 (MCT1) in the liver of pre-ruminant and adult bovines.

This study investigated the distribution and expression of monocarboxylate transporter 1 (MCT1) in the livers of pre-ruminant calves and adult bovines (bulls and cows), using different molecular biological techniques. Reverse transcription-polymerase chain reaction (RT-PCR) verified the presence of mRNA encoding for MCT1 in both pre-ruminant and adult bovine livers. Immunohistochemically, MCT1 was clearly demonstrated on the sinusoidal surfaces of bovine hepatocytes but its expression varied widely between pre-ruminants and adult bovines.

Expression and distribution of monocarboxylate transporter 1 (MCT1) in the gastrointestinal tract of calves.

In the present study the expression and distribution of monocarboxylate transporter 1 (MCT1) along the gastrointestinal tract (rumen, reticulum, omasum, abomasum, duodenum, jejunum, ileum, cecum and colon) of calves were investigated on both mRNA and protein levels. The expression of MCT1 protein and its distribution were determined by Western blotting and immunohistochemical staining, respectively by using antibody for MCT1. MCT1 protein was visualized as a 43-kDa band on immunoblots of the membrane proteins prepared from the various regions examined, and it was more highly expressed in forestomach and large intestine than in abomasum and small intestine.