Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P17931 (galectin-3)
 2,860 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A 13-month-old Korean female presented with Cushing disease and diabetes insipidus. On MRI, a 3.5-cm, focally cystic, contrast-enhancing, sellar and suprasellar mass was noted. Aside from blood adrenocorticotropin (ACTH) and cortisol elevation, other pituitary hormone blood levels were normal or markedly reduced. The subtotally resected lesion consisted of synaptophysin-immunoreactive lobules of (a) large, polygonal, amphophilic, PAS-positive cells immunoreactive for ACTH, beta-endorphin, alpha melanocyte stimulating hormone (MSH), and keratin (CAM5.2) in some cells showing Crooke hyaline change, (b) less frequent acidophilic, growth hormone (GH) immunoreactive cells, and (c) rare luteinizing hormone (LH) and/or alpha subunit immunopositive cells. Also conspicuous were smaller cells resembling Rathke-type epithelium forming rosettes to sizable glands immunoreactive for EMA, keratin, S-100 protein, galectin-3 and rarely for synaptophysin and/or one of the above-noted adenohypophysial hormones. Transcription factors, including Neuro-D1 and Pit-1, were present in ACTH- and GH-producing cells, respectively, but only in occasional Rathke-type cells. The MIB-1 labeling index (LI) was 1.5% in secretory cells and 39% in Rathke-type epithelium. Ultrastructurally, the tissue resembled fetal pituitary of 10-12 weeks gestation and contained fully differentiated corticotrophs and somatotrophs, scant cells of glycoprotein-hormone producing type with small secretory granules, and glandular epithelial cells consistent with committed, but largely undifferentiated Rathke-type epithelium. We consider the tumor as a pituitary blastoma, a lesion composed of multiple cell types common to the development of the affected organ based upon (a) prominence of primitive Rathke-type epithelium, (b) disposition of secretory cells in lobules rather than acini, (c) the limited range of secretory cells represented, (d) the presence of their corresponding transcription factors, and (e) ultrastructural features indicating orderly development of the 10- to 12-week embryonic stage.
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PMID:Pituitary blastoma. 1855 Dec 99

Spindle cell oncocytoma (SCO) of the pituitary gland is a relatively recently established, very rare subtype of adenohypophysis tumours that was introduced as a distinct clinicopathological entity in the fourth edition of WHO classification of the central nervous system tumours (2007). It is non-endocrine neoplasm of the anterior pituitary that occurs in adults and usually follows a benign clinical course, corresponding to WHO grade I. Up to now, pituitary SCO have been reported occasionally and only 14 cases of SCO have been documented in the literature. Because of their rarity, the pathogenesis and natural history of these tumours have not been fully characterized. We report two additional cases of SCO occurring in females aged 63 years (Case 1) and 65 years (Case 2), who presented with pan-hypopituitarism, headache and visual field defect. In both cases, the magnetic resonance imaging showed solid sellar mass of moderate size with suprasellar extension. The clinical and radiological features suggested non-functioning pituitary macroadenomas without evidence of invasive growth. One patient presented with tumour recurrence 3 years after undergoing the previous surgical removal of tumour, which was initially misdiagnosed as schwannoma. The first tumour was removed by transsphenoidal surgery and the second one by frontal craniotomy. Histologically and immunohistochemically, both tumours displayed the features typical for SCO of the pituitary. They were composed of interwoven fascicles of spindle cells exhibiting abundant eosinophilic cytoplasm of oncocytic or granular appearance. Mitoses were rarely observed and necrosis was absent. In one case, the advanced lymphocytic infliltration was observed within neoplastic tissue. The tumour cells exhibited immunoreactivity for S-100 protein, galectin-3, vimentin and epithelial membrane antigen but they were negative for GFAP, anterior pituitary neuroendocrine markers (prolactin, growth hormone, TSH, ACTH, FSH, LH), chromogranin, synaptophysin, cytokeratin CK (AE1/AE3), smooth muscle actin, desmin, CD34 and CD68. MIB1 labeling index did not exceed 10%. Ultrastructurally, the tumour cells were rich in mitochondria with lamellar cristae. Moreover, in Case 2 some tumour cells showed a number of giant mitochondria with severely destructed internal matrix. Spindle cell oncocytoma of the anterior pituitary is often misdiagnosed entity of uncertain histogenesis. It should be considered in the differential diagnosis of various sellar-region lesions of oncocytic morphology.
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PMID:Spindle cell oncocytoma of the adenohypophysis - a clinicopathological and ultrastructural study of two cases. 2092 1

Many newly synthesized membrane proteins traverse endocytic intermediates en route to the surface in polarized epithelial cells; however, the biosynthetic itinerary of secreted proteins has not been elucidated. We monitored the trafficking route of two secreted proteins with different apical sorting signals: the N-glycan-dependent cargo glycosylated growth hormone (gGH) and Ensol, a soluble version of endolyn whose apical sorting is independent of N-glycans. Both proteins were observed to colocalize in part with apical recycling endosome (ARE) markers. Cargo that lacks an apical targeting signal and is secreted in a nonpolarized manner did not localize to the ARE. Expression of a dominant-negative mutant of myosin Vb, which disrupts ARE export of glycan-dependent membrane proteins, selectively inhibited apical release of gGH but not Ensol. Fluorescence recovery after photobleaching (FRAP) measurements revealed that gGH in the ARE was less mobile than Ensol, consistent with tethering to a sorting receptor. However, knockdown of galectin-3 or galectin-4, lectins implicated in apical sorting, had no effect on the rate or polarity of gGH secretion. Together, our results suggest that apically secreted cargoes selectively access the ARE and are exported via differentially regulated pathways.
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PMID:Multiple biosynthetic trafficking routes for apically secreted proteins in MDCK cells. 2211 73