Worcester Foundation for Biomedical Research

About: Worcester Foundation for Biomedical Research is a based out in . It is known for research contribution in the topics: Estrone & Estrogen. The organization has 2195 authors who have published 2646 publications receiving 115809 citations. The organization is also known as: Worcester Foundation for Experimental Biology.

Spectroscopic and chemical studies of the interaction between nerve growth factor (NGF) and the extracellular domain of the low affinity NGF receptor.

Abstract: Nerve growth factor (NGF) interacts with a cell surface receptor on responsive neurons to initiate a series of cellular events leading to neuronal survival and/or differentiation. The first step in this process is the binding of NGF to a low affinity and/or a high affinity receptor. In the present report, we have studied the conformation and stability of recombinant receptor extracellular domain (RED) from the human low affinity receptor and the structural basis of its interaction with NGF. Circular dichroism (CD) studies indicate that the RED is primarily random coil in nature with little regular secondary structure. Thermal stability studies have shown that this irregular conformation is a specific structure that can undergo a reversible two-state thermal denaturation with a concomitant fluorescent and CD change. During heating at 100 degrees C for 15 min, the structure of RED is sufficiently unfolded for a reducing agent, dithiothreitol, to inactivate the receptor toward NGF binding and cross-linking. The complex formation between the RED and NGF has been examined by differential CD measurements, and we have shown that a small, reproducible change in conformation occurs in RED or NGF upon interaction. These results are interpreted in terms of the initiation of NGF cell surface binding and possible modes of signal transduction.

Ci, STEROIDS, 17a-HYDROXYCORTICOSTERONE AND A SODIUM RETAINING FACTOR IN HUMAN FETAL ADRENAL GLANDS1

Abstract: THE embryological development of the human fetal adrenal cortex, and, perhaps, other primates, is unique. During the second month of fetal life, a distinct adrenal cortex is recognized. It reaches its largest relative size during the third and fourth month when it occupies about 0.5% of the total body volume as compared to 0.01% in the adult (Jackson, 1909). The histological picture of the fetal adrenal cortex differs from that of the adult by the presence of the fetal zone, which comprises about 80% of the whole cortex. The fetal zone degenerates rapidly during the first post-natal months. In addition, only the glomerular and fascicular zones of the cortex are fairly well developed in the fetus (Lanman, 1953). In contrast to the available data on the morphology and anatomy of the human fetal adrenal cortex, its physiology remains largely unknown. An excellent review of the subject has been published by Lanman (1953). Large amounts of ascorbic acid (Bourne, 1933) and lipid material (Lanman, 1953) have bee...

Progestational activity of certain 19-norsteroids and progesterone derivatives.

Abstract: Seven 19-norsteroids, 17α-ethinyl-19-nortestosterone (I), 17α-ethinyl-5(10)-estraenolone (II), 17α-ethyl-19-nortestosterone (III), 17α-methyl-19-nortestosterone (IV), 17α-propyl-l9-nortestosterone (V), 17α-butenyl-19-nortestosterone (VI), and 17α-allyl-19-nortestosterone (VII), and two progesterone derivatives—17α-hydroxyprogesterone-17-acetate (VIII) and 17α-hydroxy- 6α-methyl-progesterone acetate (IX) have beenadministered subcutaneously or orally into Clauberg rabbits to demonstj-ate their progestational activity by estimation of endometrial carbonic anhydrase content and measurement of the uterine G/M ratio. The increase of endometrial carbonic anhydrase content induced by treatment with each compoundcorrelates well with that of the G/M ratio which measures uterine proliferation. Similarly, the relative potencies by the enzyme test correspond to those obtained by the G/M assay either in subcutaneous treatment or in oral administration. The relationship between the progestational activity and the lengt...

An alternatively spliced form of the transcription factor Sp1 containing only a single glutamine-rich transactivation domain.

Abstract: Protein-protein interactions involving specific transactivation domains play a central role in gene transcription and its regulation. The promoter-specific transcription factor Sp1 contains two glutamine-rich transcriptional activation domains (A and B) that mediate direct interactions with the transcription factor TFIID complex associated with RNA polymerase II and synergistic effects involving multiple Sp1 molecules. In the present study, we report the complementary DNA sequence for an alternatively spliced form of mouse Sp1 (mSp1-S) that lacks one of the two glutamine-rich activation regions present in the full-length protein. Corresponding transcripts were identified in mouse tissues and cell lines, and an Sp1-related protein identical in size to that predicted for mSp1-S was detected in mouse nuclear extracts. Cotransfection analysis revealed that mSp1-S lacks appreciable activity at promoters containing a single Sp1 response element but is active when multiple Sp1 sites are present, suggesting synergistic interactions between multiple mSp1-S molecules. The absence of a single glutamine-rich domain does not fully explain the properties of the smaller protein and indicates that additional structural features account for its unique transcriptional activity. The functional implications of this alternatively spliced form of Sp1 are discussed.