TOXOHORMONE IN BACTERIA-FREE TUMORS

1966 ◽  
Vol 44 (8) ◽  
pp. 1069-1087 ◽  
Author(s):  
J. C. Nixon ◽  
B. Zinman
Keyword(s):  
Gel Filtration ◽  
Human Kidney ◽  
Metastatic Carcinoma ◽  
Exchange Chromatography ◽  
Human Spleen ◽  
Normal Tissues ◽  
Highly Active ◽  
Normal Human Kidney ◽  
Tumor Tissues ◽  
Normal Human

Toxohormone was extracted from bacteria-free human tumors and normal tissues, and assayed for activity by measuring the decrease in serum iron levels of rats 12 hours after injection of the extracts. In contrast with the findings of others, the results of the present study demonstrated that active toxohormone could be isolated from bacteria-free tumor tissues. Bacteria-free normal human kidney and spleen also yielded active toxohormone extracts, whereas extracts of normal human- and rat-skeletal muscle and rat liver had no activity.Four active toxohormone extracts were purified by ion-exchange chromatography followed by gel filtration. Human leukemic spleen, metastatic carcinoma of the cecum, and normal human spleen and kidney yielded several highly active purified fractions.

scholarly journals Biosynthesis of Complement C4 Messenger RNA in Normal Human Kidney

Nephron ◽  
1989 ◽  
Vol 53 (4) ◽  
pp. 338-342 ◽  
Author(s):  
H.E. Feucht ◽  
J. Zwirner ◽  
D. Bevec ◽  
Margot Lang ◽  
E. Felber ◽  
...  
Keyword(s):  
Messenger Rna ◽  
Human Kidney ◽  
Complement C4 ◽  
Normal Human Kidney ◽  
Normal Human

scholarly journals Different expression of the plasminogen activation system in renal thrombotic microangiopathy and the normal human kidney

1996 ◽  
Vol 50 (6) ◽  
pp. 2011-2019 ◽  
Author(s):  
Yichun Xu ◽  
Jacqueline Hagege ◽  
Béatrice Mougenot ◽  
Jean-Daniel Sraer ◽  
Ebbe Rønne ◽  
...  
Keyword(s):  
Thrombotic Microangiopathy ◽  
Human Kidney ◽  
Plasminogen Activation ◽  
Plasminogen Activation System ◽  
Normal Human Kidney ◽  
Activation System ◽  
Normal Human

scholarly journals Cellular receptors for matrix proteins in normal human kidney and human mesangial cells

1990 ◽  
Vol 38 (5) ◽  
pp. 886-895 ◽  
Author(s):  
Fernando G. Cosio ◽  
Daniel D. Sedmak ◽  
N. Stanley Nahman
Keyword(s):  
Mesangial Cells ◽  
Human Kidney ◽  
Matrix Proteins ◽  
Cellular Receptors ◽  
Human Mesangial Cells ◽  
Normal Human Kidney ◽  
Normal Human

scholarly journals Human ADPKD primary cyst epithelial cells with a novel, single codon deletion in the PKD1 gene exhibit defective ciliary polycystin localization and loss of flow-induced Ca2+ signaling

2007 ◽  
Vol 292 (3) ◽  
pp. F930-F945 ◽  
Author(s):  
Chang Xu ◽  
Sandro Rossetti ◽  
Lianwei Jiang ◽  
Peter C. Harris ◽  
Ursa Brown-Glaberman ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Nk Cells ◽  
Coiled Coil ◽  
Human Kidney ◽  
Coiled Coil Domain ◽  
Normal Human Kidney ◽  
Cyst Cells ◽  
Localization Signal ◽  
Normal Human ◽  
Autosomal Dominant Polycystic Kidney

Autosomal dominant polycystic kidney disease (ADPKD) gene products polycystin-1 (PC1) and polycystin-2 (PC2) colocalize in the apical monocilia of renal epithelial cells. Mouse and human renal cells without PC1 protein show impaired ciliary mechanosensation, and this impairment has been proposed to promote cystogenesis. However, most cyst epithelia of human ADPKD kidneys appear to express full-length PC1 and PC2 in normal or increased abundance. We show that confluent primary ADPKD cyst cells with the novel PC1 mutation ΔL2433 and with normal abundance of PC1 and PC2 polypeptides lack ciliary PC1 and often lack ciliary PC2, whereas PC1 and PC2 are both present in cilia of confluent normal human kidney (NK) epithelial cells in primary culture. Confluent NK cells respond to shear stress with transient increases in cytoplasmic Ca2+ concentration ([Ca2+]i), dependent on both extracellular Ca2+ and release from intracellular stores. In contrast, ADPKD cyst cells lack flow-sensitive [Ca2+]i signaling and exhibit reduced endoplasmic reticulum Ca2+ stores and store-depletion-operated Ca2+ entry but retain near-normal [Ca2+]i responses to ANG II and to vasopressin. Expression of wild-type and mutant CD16.7-PKD1(115–226) fusion proteins reveals within the COOH-terminal 112 amino acids of PC1 a coiled-coil domain-independent ciliary localization signal. However, the coiled-coil domain is required for CD16.7-PKD1(115–226) expression to accelerate decay of the flow-induced Ca2+ signal in NK cells. These data provide evidence for ciliary dysfunction and polycystin mislocalization in human ADPKD cells with normal levels of PC1.

scholarly journals Mapping of Carboxypeptidase M in Normal Human Kidney and Renal Cell Carcinoma

2012 ◽  
Vol 61 (3) ◽  
pp. 218-235 ◽  
Author(s):  
Catherine J. Denis ◽  
Nathalie Van Acker ◽  
Stefanie De Schepper ◽  
Martine De Bie ◽  
Luc Andries ◽  
...  
Keyword(s):  
Renal Cell Carcinoma ◽  
Cell Carcinoma ◽  
Renal Cell ◽  
Human Kidney ◽  
Normal Human Kidney ◽  
Normal Human ◽  
Carboxypeptidase M

The Effect of Uninephrectomy on Mineral Metabolism in Normal Human Kidney Donors

1988 ◽  
Vol 11 (5) ◽  
pp. 393-401 ◽  
Author(s):  
Miriam A. Friedlander ◽  
Jon H. Lemke ◽  
Ronald L. Horst
Keyword(s):  
Mineral Metabolism ◽  
Human Kidney ◽  
Kidney Donors ◽  
Normal Human Kidney ◽  
Normal Human

scholarly journals Expression of Silencer of Death Domains and Death-Receptor-3 in Normal Human Kidney and in Rejecting Renal Transplants

2003 ◽  
Vol 163 (2) ◽  
pp. 401-411 ◽  
Author(s):  
Rafia S. Al-Lamki ◽  
Jun Wang ◽  
Sathia Thiru ◽  
Nicholas R. Pritchard ◽  
J. Andrew Bradley ◽  
...  
Keyword(s):  
Death Receptor ◽  
Human Kidney ◽  
Renal Transplants ◽  
Normal Human Kidney ◽  
Normal Human ◽  
Death Receptor 3

Bone morphogenetic proteins -2, -4, -6, -7 and their receptors are expressed in normal human kidney and renal cell carcinoma

Bone ◽  
2010 ◽  
Vol 47 ◽  
pp. S109
Author(s):  
D. Markic ◽  
T. Celic ◽  
J. Spanjol ◽  
A. Grskovic ◽  
Z. Fuckar ◽  
...  
Keyword(s):  
Renal Cell Carcinoma ◽  
Cell Carcinoma ◽  
Bone Morphogenetic Proteins ◽  
Renal Cell ◽  
Human Kidney ◽  
Normal Human Kidney ◽  
Normal Human
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