Biomedical subjects

Xiao-Ming Zhu

Publications and source records attributed to Xiao-Ming Zhu.

3 recordsLinked to original sources

PubMed2004

Changes in GABA transporters in the rat hippocampus after kainate-induced neuronal injury: decrease in GAT-1 and GAT-3 but upregulation of betaine/GABA transporter BGT-1.

The gamma-aminobutyric acid (GABA) transporters GAT-1, GAT-2, GAT-3, and BGT-1 have been cloned and identified according to their differential amino acid sequences and pharmacologic properties. In contrast to GAT-1, -2, or -3, BGT-1 is capable of utilizing both GABA and betaine as substrates. Betaine has been suggested to be a protective osmolyte in the brain. Because changes in expression of GABA transporters/BGT-1 might result in alterations in levels of GABA/betaine in the extracellular space, with consequent effects on neuronal excitability or osmolarity, the present study was carried out to explore expression of GABA transporters in the rat hippocampus after kainate-induced neuronal injury. A decrease in GAT-1 and GAT-3 immunostaining but no change in GAT-2 staining was observed in the degenerating CA subfields. In contrast, increased BGT-1 immunoreactivity was observed in astrocytes after kainate injection. BGT-1 is a weak transporter of GABA in comparison to other GABA transporters and the increased expression of BGT-1 in astrocytes might be a protective mechanism against increased osmotic stress known to occur after excitotoxic injury. On the other hand, excessive or prolonged BGT-1 expression might be a factor contributing to astrocytic swelling after brain injury.

Animals↗

PubMed2004

A light and electron microscopic study of betaine/GABA transporter distribution in the monkey cerebral neocortex and hippocampus.

The present study aimed to elucidate the distribution of betaine/gamma-aminobutyric acid (GABA) transporter-1 (BGT-1) in the normal monkey cerebral neocortex and hippocampus by immunoperoxidase and Immunogold labelling. BGT-1 was observed in pyramidal neurons in the cerebral neocortex and the CA fields of the hippocampus. Large numbers of small diameter dendrites or dendritic spines were observed in the neuropil. These made asymmetrical synaptic contacts with unlabelled axon terminals containing small round vesicles, characteristic of glutamatergic terminals. BGT-1 label was observed in an extra-perisynaptic region, away from the post-synaptic density. Immunoreactivity was not observed in portions of dendrites that formed symmetrical synapses, axon terminals, or glial cells. The distribution of BGT-1 on dendritic spines, rather than at GABAergic axon terminals, suggests that the transporter is unlikely to play a major role in terminating the action of GABA at a synapse. Instead, the osmolyte betaine is more likely to be the physiological substrate of BGT-1 in the brain, and the presence of the transporter in pyramidal neurons suggests that these neurons utilize betaine to maintain osmolarity.

Animals↗

PubMed2003

Multi-factorial role of GnRH-I and GnRH-II in the human ovary.

Normal ovarian functions are regulated by a wide variety of endocrine hormones, local paracrine and autocrine factors, which functionally interact with each other in a highly coordinated fashion. Recent findings have demonstrated that both forms of gonadotropin-releasing hormone (GnRH-I and GnRH-II) are expressed in various compartments of the human ovary including the granulosa-luteal cells, ovarian surface epithelial cells and ovarian tumors, and their expressions have been shown to be tightly regulated by gonadal steroids and gonadotropins. Functionally, these neuropeptides exert diverse biological effects in the ovary via binding to their cognate receptors, supporting the notion that these peptides act as paracrine and autocrine factors in modulating local ovarian functions. In this review, we will summarize recent literatures regarding the regulation of GnRH-I and GnRH-II gene expressions in the human ovary, and discuss the possible signal transduction mechanisms by which these hormones exert their actions in the gonad. Recent cloning of the second form of the GnRH receptor (GnRH-II receptor) in primates and other vertebrates demonstrated that it was structurally, and thus, functionally distinct from the GnRH-I receptor. Cell proliferation studies showed that GnRH-II inhibited the growth of human ovarian cancer cells that express GnRH-II but not GnRH-I receptor, indicating that the GnRH-II binding sites are functional in these cells. However, it remains unknown if GnRH-II receptor is expressed as a full-length, properly processed and functional gene transcript in humans, and its potential physiological roles such as differential regulation of gonadotropin secretion, neuroendocrine modulation and female sexual behavior await further investigation.

Amino Acid Sequence↗