Immunohistochemical identification and characterization of a special type of desmin-producing stromal cells in human placenta and other fetal tissues

1994 ◽  
Vol 56 (3) ◽  
pp. 191-199 ◽  
Author(s):  
Harald G. Sparn ◽  
Brigitte A. Lieder-Ochs ◽  
Werner W. Franke
Keyword(s):  
Human Placenta ◽  
Stromal Cells ◽  
Fetal Tissues ◽  
Identification And Characterization ◽  
Immunohistochemical Identification

Identification and characterization of a corticotrophin-releasing hormone receptor in human placenta

1995 ◽  
Vol 133 (5) ◽  
pp. 591-597 ◽  
Author(s):  
Vicki L Clifton ◽  
Phillip C Owens ◽  
Phillip J Robinson ◽  
Roger Smith
Keyword(s):  
Human Placenta ◽  
Binding Sites ◽  
Hormone Receptor ◽  
Human Myometrium ◽  
Scatchard Analysis ◽  
Releasing Hormone ◽  
Rat Pituitary ◽  
Identification And Characterization ◽  
Crh Receptors

Clifton VL, Owens PC, Robinson PJ, Smith R. Identification and characterization of a corticotrophinreleasing hormone receptor in human placenta. Eur J Endocrinol 1995;133:591–7. ISSN 0804–4643 Corticotrophin-releasing hormone (CRH) causes vasodilatation in the human fetal–placental circulation and has paracrine actions in placental tissue, suggesting that CRH receptors may be present in the human placenta. We have now identified and characterized placental CRH binding sites and compared them to those described previously in human myometrium and rat pituitary. Radiolabelled ovine CRH binding to placental membranes was pH-, time-, temperature- and divalent cation-dependent and was reversible in the presence of 1 μmol/l unlabelled ovine CRH. Scatchard analysis of placentae delivered vaginally or by elective caesarean section revealed dissociation constants (Kd) of 214.5 ± 84 pmol/l (N = 8) and 45.4 ± 23.9 pmol/l (N = 9), respectively. The Kd for caesarean placental binding sites was similar to that of human myometrium (59.6 pmol/l, N = 3) and rat pituitary (82.5 pmol/l, N = 3) receptors. However, in vaginally delivered placentae the CRH binding sites had a much lower affinity (p < 0.05). The receptor densities (Bmax) of vaginally delivered and caesarean-delivered placentae were 28.6 ± 9.6 and 6.1 ± 2.8 fmol/mg, respectively (p < 0.05). Chemical cross-linking studies using disuccinimidyl suberate indicated that the molecular weight of the CRH receptor in the placenta and rat pituitary is 75 kD. We conclude that there is a high-affinity population of CRH binding sites in the human placenta that are physicochemically similar to pituitary and myometrial CRH receptors. The CRH receptor properties in the placenta change in response to labour, when CRH levels in maternal blood are highest, suggesting that placental CRH may regulate its receptor. R Smith, Endocrinology Unit, John Hunter Hospital, Locked Bag 1, Hunter Regional Mail Centre, Newcastle, NSW 2310, Australia

Characterization of extracellular vesicles derived from two populations of human placenta derived mesenchymal stem/stromal cells

Cytotherapy ◽  
2020 ◽  
Vol 22 (5) ◽  
pp. S50
Author(s):  
R. Khanabdali ◽  
M. Shojaee ◽  
J. Johnson ◽  
S. Law ◽  
M. Whitmore ◽  
...  
Keyword(s):  
Extracellular Vesicles ◽  
Human Placenta ◽  
Stromal Cells ◽  
Two Populations

scholarly journals Identification and Characterization of Human Endometrial Mesenchymal Stem/Stromal Cells and Their Potential for Cellular Therapy

2016 ◽  
Vol 5 (9) ◽  
pp. 1127-1132 ◽  
Author(s):  
Saeedeh Darzi ◽  
Jerome A. Werkmeister ◽  
James A. Deane ◽  
Caroline E. Gargett
Keyword(s):  
Stromal Cells ◽  
Cellular Therapy ◽  
Identification And Characterization

scholarly journals Identification and characterization of mature β-hexosaminidases associated with human placenta lysosomal membrane

2008 ◽  
Vol 28 (4) ◽  
pp. 229-237 ◽  
Author(s):  
Alessandro Magini ◽  
Simona Mencarelli ◽  
Brunella Tancini ◽  
Virginia Ciccarone ◽  
Lorena Urbanelli ◽  
...  
Keyword(s):  
Human Placenta ◽  
Lysosomal Membrane ◽  
Testable Hypothesis ◽  
Gm2 Ganglioside ◽  
Hydrophilic Nature ◽  
Peripheral Membrane Protein ◽  
Triton X ◽  
Identification And Characterization ◽  
Dimensional Electrophoresis

Hex (β-hexosaminidase) is a soluble glycohydrolase involved in glycoconjugate degradation in lysosomes, however its localization has also been described in the cytosol and PM (plasma membrane). We previously demonstrated that Hex associated with human fibroblast PM as the mature form, which is functionally active towards GM2 ganglioside. In the present study, Hex was analysed in a lysosomal membrane-enriched fraction obtained by purification from highly purified human placenta lysosomes. These results demonstrate the presence of mature Hex associated with the lysosomal membrane and displaying, as observed for the PM-associated form, an acidic optimum pH. When subjected to sodium carbonate extraction, the enzyme behaved as a peripheral membrane protein, whereas Triton X-114 phase separation confirmed its partially hydrophilic nature, characteristics which are shared with the PM-associated form of Hex. Moreover, two-dimensional electrophoresis indicated a slight difference in the pI of β-subunits in the membrane and the soluble forms of the lysosomal Hex. These results reveal a new aspect of Hex biology and suggest that a fully processed membrane-associated form of Hex is translocated from the lysosomal membrane to the PM by an as yet unknown mechanism. We present a testable hypothesis that, at the cell surface, Hex changes the composition of glycoconjugates that are known to be involved in intercellular communication and signalling.

scholarly journals Identification and characterization of a rich population of CD34+ mesenchymal stem/stromal cells in human parotid, sublingual and submandibular glands

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Padma Priya Togarrati ◽  
Robson T. Sasaki ◽  
Mohamed Abdel-Mohsen ◽  
Nuntana Dinglasan ◽  
Xutao Deng ◽  
...  
Keyword(s):  
Stromal Cells ◽  
Submandibular Glands ◽  
Identification And Characterization

scholarly journals Downregulated Expression of Ly-6-ThB on Developing T Cells Marks CD4+CD8+Subset Undergoing Selection in the Thymus

2001 ◽  
Vol 8 (2) ◽  
pp. 107-121 ◽  
Author(s):  
Justin T. Reese ◽  
Hitesh Mehta ◽  
Clay H. Chappell ◽  
Anil. Bamezai
Keyword(s):  
T Cells ◽  
Stromal Cells ◽  
Negative Selection ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Thymic Selection ◽  
Cd8 Cell ◽  
Peptide Complexes ◽  
Identification And Characterization

Interaction of TCRs on CD4+CD8+immature T cell with MHC-peptide complexes on stromal cells is required for positive and negative selection in the thymus. Identification and characterization of a subpopulation of CD4+CD8+thymocytes undergoing selection in the thymus will aid in understanding the mechanisms underlying lineage commitment and thymic selection. Herein, we describe the expression of Ly-6 ThB on developing thymocytes. The majority of CD4+CD8+thymocytes express Ly-6 ThB at high levels. Its expression is downregulated in a subset of CD4+CD8+thymocytes as well as in mature CD4+CD8-and CD4-CD8+T cells. More importantly, interaction of TCR/coreceptor with the self-MHC-peptide contributes to the downregulation of ThB expression on developing thymocytes. These findings indicate that downregulation of ThB on CD4+CD8+thymocytes identifies a unique subset (CD4+CD8+ThBneg–low) of thymocytes that has received the initial signals for thymic selection but have not yet downregulated the CD4 and CD8 cell surface expression. In addition, these results also indicate that a high frequency (Ÿ20–40%) of CD4+CD8+immature thymocytes receive these initial signals during thymic selection.

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