scholarly journals Heterogeneous Expression of Chondroitin Sulfate Glycosaminoglycans and Versican Proteoglycan during Early Development of Rathke’s Pouch

2014 ◽  
Vol 2014 ◽  
pp. 1-11
Author(s):  
Sheelah Iyengar ◽  
Anthony A. Capehart
Keyword(s):  
Basement Membrane ◽  
Chondroitin Sulfate ◽  
Anterior Pituitary ◽  
Rathke’S Pouch ◽  
Rathke's Pouch ◽  
Asymmetric Pattern ◽  
Heterogeneous Expression ◽  
Morphogenetic Factors ◽  
Strong Staining ◽  
Ventral Diencephalon

While much is known regarding morphogenetic factors involved in specification and differentiation of Rathke’s pouch, less attention has been given to extracellular matrix (ECM) interactions involved in its formation. The present research investigated localization of two different chondroitin sulfate glycosaminoglycans (CS-GAGs), TC2 and d1C4, and versican CS-proteoglycan (PG) to identify additional ECM molecules involved in formation of the pituitary rudiment. Immunohistochemical evaluation of anterior pituitary primordia between HH15 and HH28 showed these ECM molecules prevalent in basement membrane and surrounding ECM underlying Rathke’s epithelia and to a lesser extent between pouch epithelial cells. TC2/d1C4 CS-GAGs and versican showed changing and heterogeneous localization during pouch development that suggested specific roles in cell-ECM interaction during pituitary morphogenesis. TC2 antigen colocalized with versican at early stages in an asymmetric pattern, with particularly strong staining between ventral diencephalon and roof of Rathke’s pouch while d1C4 CS-GAG encompassed the entire pouch by HH22 indicating association with a different CSPG. The heparan sulfate proteoglycan, perlecan, used to verify basement membrane structure, was a consistent component of Rathke’s pouch. Data show a dynamic and heterogeneous pattern of CS-GAG and versican expression during early chick Rathke’s pouch development that suggests new possibilities for ECM function in its establishment and growth.

scholarly journals Role of PROP1 in Pituitary Gland Growth

2005 ◽  
Vol 19 (3) ◽  
pp. 698-710 ◽  
Author(s):  
Robert D. Ward ◽  
Lori T. Raetzman ◽  
Hoonkyo Suh ◽  
Brandon M. Stone ◽  
Igor O. Nasonkin ◽  
...  
Keyword(s):  
Pituitary Gland ◽  
Anterior Pituitary ◽  
Anterior Lobe ◽  
Clinical Findings ◽  
Proliferative Potential ◽  
Rathke’S Pouch ◽  
Rathke's Pouch ◽  
Pituitary Hyperplasia ◽  
Dividing Cells ◽  
Pituitary Hypoplasia

Abstract Mutations in the PROP1 transcription factor gene lead to reduced production of thyrotropin, GH, prolactin, and gonadotropins as well as to pituitary hypoplasia in adult humans and mice. Some PROP1-deficient patients initially exhibit pituitary hyperplasia that resolves to hypoplasia. To understand this feature and to explore the mechanism whereby PROP1 regulates anterior pituitary gland growth, we carried out longitudinal studies in normal and Prop1-deficient dwarf mice from early embryogenesis through adulthood, examining the volume of Rathke’s pouch and its derivatives, the position and number of dividing cells, the rate of apoptosis, and cell migration by pulse labeling. The results suggest that anterior pituitary progenitors normally leave the perilumenal region of Rathke’s pouch and migrate to form the anterior lobe as they differentiate. Some of the cells that seed the anterior lobe during organogenesis have proliferative potential, supporting the expansion of the anterior lobe after birth. Prop1-deficient fetal pituitaries are dysmorphic because mutant cells are retained in the perilumenal area and fail to differentiate. After birth, mutant pituitaries exhibit enhanced apoptosis and reduced proliferation, apparently because the mutant anterior lobe is not seeded with progenitors. These studies suggest a mechanism for Prop1 action and an explanation for some of the clinical findings in human patients.

scholarly journals cDNA Cloning of the Basement Membrane Chondroitin Sulfate Proteoglycan Core Protein, Bamacan: A Five Domain Structure Including Coiled-Coil Motifs

1997 ◽  
Vol 136 (2) ◽  
pp. 433-444 ◽  
Author(s):  
Rong-Rong Wu ◽  
John R. Couchman
Keyword(s):  
Basement Membrane ◽  
Chondroitin Sulfate ◽  
Core Protein ◽  
Coiled Coil ◽  
Basement Membranes ◽  
Cdna Clones ◽  
Molecular Architecture ◽  
Unusual Structure ◽  
Extracellular Matrix Molecule

Basement membranes contain several proteoglycans, and those bearing heparan sulfate glycosaminoglycans such as perlecan and agrin usually predominate. Most mammalian basement membranes also contain chondroitin sulfate, and a core protein, bamacan, has been partially characterized. We have now obtained cDNA clones encoding the entire bamacan core protein of Mr = 138 kD, which reveal a five domain, head-rod-tail configuration. The head and tail are potentially globular, while the central large rod probably forms coiled-coil structures, with one large central and several very short interruptions. This molecular architecture is novel for an extracellular matrix molecule, but it resembles that of a group of intracellular proteins, including some proposed to stabilize the mitotic chromosome scaffold. We have previously proposed a similar stabilizing role for bamacan in the basement membrane matrix. The protein sequence has low overall homology, apart from very small NH2- and COOH-terminal motifs. At the junctions between the distal globular domains and the coiled-coil regions lie glycosylation sites, with up to three N-linked oligosaccharides and probably three chondroitin chains. Three other Ser-Gly dipeptides are unfavorable for substitution. Fusion protein antibodies stained basement membranes in a pattern commensurate with bamacan, and they also Western blotted bamacan core protein from rat L2 cell cultures. The antibodies could also specifically immunoprecipitate an in vitro transcription/translation product from a full-length bamacan cDNA. The unusual structure of this proteoglycan is indicative of specific functional roles in basement membrane physiology, commensurate with its distinct expression in development and changes in disease models.

Enhancement of the Canonical Wnt Pathway in Rathke's Pouch Results in Pituitary Tumours Reminiscent of Human Adamantinomatous Craniopharyngioma.

2010 ◽  
pp. OR38-3-OR38-3
Author(s):  
Carles Gaston-Massuet ◽  
Cynthia L Andoniadou ◽  
Massimo Signore ◽  
Sajutha Jayakody ◽  
Nicoletta Charolidi ◽  
...  
Keyword(s):  
Wnt Pathway ◽  
Pituitary Tumours ◽  
Rathke’S Pouch ◽  
Rathke's Pouch ◽  
Canonical Wnt Pathway ◽  
Adamantinomatous Craniopharyngioma ◽  
Canonical Wnt

Rathke's pouch morphogenesis in the chick embryo

1979 ◽  
Vol 207 (3) ◽  
pp. 351-366 ◽  
Author(s):  
Antone G. Jacobson ◽  
David M. Miyamoto ◽  
S.-H. Mai
Keyword(s):  
Chick Embryo ◽  
Rathke’S Pouch ◽  
Rathke's Pouch

Sellar enlargement with hyperprolactinemia and a Rathke's pouch cyst

JAMA ◽  
1978 ◽  
Vol 240 (5) ◽  
pp. 471-473 ◽  
Author(s):  
K. M. Trokoudes
Keyword(s):  
Rathke’S Pouch ◽  
Rathke's Pouch

scholarly journals Retinoic acid is required for specification of the ventral eye field and for Rathke's pouch in the avian embryo

2007 ◽  
Vol 51 (3) ◽  
pp. 191-200 ◽  
Author(s):  
Malcolm Maden ◽  
Aida Blentic ◽  
Susan Reijntjes ◽  
Sophie Seguin ◽  
Emily Gale ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Avian Embryo ◽  
Rathke’S Pouch ◽  
Rathke's Pouch ◽  
Eye Field
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