Bone-Induced Her2 Promotes Secondary Metastasis in HR+/Her2- Breast Cancer.

Bone metastases can disseminate to secondary sites and promote breast cancer progression creating additional clinical challenges. The mechanisms contributing to secondary metastasis are barely understood. Here, we evaluate the prediction power of Her2-expressing (Her2E) circulating tumor cells (CTCs) after analyzing over 13,000 CTCs from a cohort of 137 metastatic breast cancer (MBC) patients with initial HR+/Her2- status and employ preclinical models of bone metastasis (BM) to validate the role of Her2E CTCs in multi-organ metastases.

New York City's Community-Based Organizations and the COVID-19 Pandemic: A Descriptive Analysis of Local Organizations' Response Efforts and Their Role During Public Health Crises.

Community-based organizations (CBOs) are on the frontlines offering resources and support to residents during times of distress. Through a community-academic partnership, an interdisciplinary team developed, collected, and analyzed 91 surveys from social services providers across New York City assessing the impact of the COVID-19 pandemic on their organizations' operations. The majority (93%) of these organizations stayed open during the pandemic but had to shift the services they offered to meet new needs.

Methyltransferases of gentamicin biosynthesis.

Gentamicin C complex from remains a globally important antibiotic, and there is revived interest in the semisynthesis of analogs that might show improved therapeutic properties. The complex consists of five components differing in their methylation pattern at one or more sites in the molecule. We show here, using specific gene deletion and chemical complementation, that the gentamicin pathway up to the branch point is defined by the selectivity of the methyltransferases GenN, GenD1, and GenK.

[The effect of chronic x-ray radiation at low doses on the gamma-glutamyl transpeptidase activity in rat organs and tissues].

Effect of chronic low dose X-ray irradiation (total doses of 2.58, 5.16, 6.

[The glutathione content and glutathione-S-transferase activity in the organs and blood of rats following chronic irradiation at low doses].

The effect of chronic low dose-rate irradiation with X-rays up to total doses of 2.58, 5.16, 6.

[The effect of x-ray radiation and hypoxia on the proteolytic activity of the normal rat spleen and during tumor growth].

The influence of X-radiation on activity of lysosomal enzymes (D, L, H cathepsins) in rat spleen tissue and in inoculated rat sarcoma 45 has been investigated. Intact rats and rats with tumors were subjected to whole-body and sarcoma 45 to local irradiation with doses of 0.155 C/kg and 0.

[An increase in the brain homocarnosine level during alcohol intoxication].

It is shown that the content of neurospecific dipeptide of homocarnosine in the brain and blood of rats increases considerably after intraperitoneal administration of ethanol. The exogenous leu-enkephalin exerts an effects on the development of the alcoholic organism response.

[Cathepsin H activity in the human brain and human brain neoplasms].

The human brain cathepsin H is shown to be a specific cysteine aminopeptidase with the optimum activity at pH 6.0. Human brain tumours of neuroectodermal (astrocytomas and glioblastomas) and epithelial (meningiomas) origin were used to study the cathepsin H activity in the malignant brain tissue.

[Ammonia content of the brain, liver and blood of rats in radiation injury].

The neuroparalytic syndrome induced by ammonia was compared with the X-radiation-induced cerebral syndrome. It is suggested that the accumulation of ammonia in the brain and liver of rats is one of the reasons for the similarity of the studied syndromes. The fact that ammonia is bound by glutamic acid indicates that the latter is involved in the mechanisms of ammonia utilization and in the radioprotective properties manifestation.

[Characteristics of various nerve tissue proteins using group-specific sorbents].

The use of micro-scale column chromatography and affinity immunoelectrophoresis with group-specific sorbents allows studying some physical and chemical properties of protein molecules. A comparison of properties of soluble and membrane brain amino-peptidases carried out by means of micro-scale phenyl-sepharose and ConA-sepharose column chromatography shows that the membrane-bound aminopeptidase is a glycoprotein which possesses a high capacity to hydrophobic interactions. Soluble forms of aminopeptidase do not interact with ConA or phenyl residues.

[Immunochemical study of the degradation of circulating glycoproteins and the neurospecific membrane glycoprotein D2 by cathepsin D of the human brain].

Cathepsin D was isolated from human brain. A consecutive use of affinity chromatography on hemoglobin-sepharose 4B and column chromatography on hydroxylapatite resulted in a homogeneous enzyme (as was demonstrated by SDS polyacrylamide gel electrophoresis) with a molecular weight of about 48,000, 2800-fold purification and 3.4% yield.

[Effect of hypothermia on subcellular distribution and various physico-chemical properties of cathepsin D in rat brain].

The total cooling ef rats down to the rectal temperature 30 degrees and 20 degrees C does not change significantly the ratio of the relative specific activity of cathepsin D in subcellular fractions of the rat brain. The gel chromatographic analysis of heterogeneity of cathepsin D molecular forms in subcellular fractions established the presence of a high-molecular (in the fractions of lysosome and microsome mitochondria) and a low-molecular (in the fractions of lysosome and cytosol mitochondria) enzyme forms. Under hypothermia (20 degrees C) in the brain cytosol fraction there arises a minor zone of the cathepsin D activity corresponding to the high-molecular enzyme form.

[Glycyl-glycine dipeptidase from cat nervous tissue].

The local distribution of glycyl-glycine dipeptidase (EC 3.4.13.

[Purification and properties of thiol-activated cathepsin from bovine cerebrum and cerebellum].

Thiol-activated cathepsin was isolated from bovine cerebral hemispheres and cerebellum. The enzyme from the hemispheres was purified by the affinity sorbent chromatography method with the sepharose-4B-immobilized protein substrate, azocasein, and with subsequent separation of nonspecifically sorbed protein by column gel-chromatography on Sephadex G-100. The cathepsin pH-optimum was 6.

[Purification and properties of inhibitor from vegetative portion of alfalfa].

Trypsin inhibitor was isolated from the vegetative portion of alfalfa and purified 270-fold by affinity chromatography on Trypsin-Sepharose. The inhibitor was eluted by gel-filtration as a single peak with molecular weight of 6900. Disc-electrophoresis of the purified inhibitor revealed the presence of only one protein band.

[Catalytic properties of cathepsin D from the brains of normal and irradiated animals].

Biospecific sorbent, hemoglobin-biogel P-300, was used for purification of cathepsin D from the brain and spleen of a cat and from the brain of normal and irradiated rats. 800 R irradiation of rats in 7 days causes changes in the catalytic properties of cathepsin D: shift of the pH-optimum of the activity, increase in the enzyme affinity to the substrate (hemoglobin) and inhibitor (pepstatin), changes in the activation energy. These changes may be due to the destruction of the processes of posttranscriptional modification of the enzymes at the late stage of the radiation pathology.

[Isolation and purification of bovine and porcine cerebral cathepsin D].

Cathepsin D was isolated from the grey matter of bovine and porcine large cerebral hemispheres and purified by affinity chromatography on haemoglobin--Sepharose. The isolation and purification of the enzyme also included: acidic extraction, precipitation by ammonium sulfate, dialysis, affinity chromatography, concentration and gel-chromatography on Sephadex G-100. The degree of purification of bovine cerebral enzyme was 3280.

[Cathepsin B1 activity in cat brain tissue].

The dependence of the cathepsin B1 (EC 3.4.22.

[Molecular forms of acid proteinases of the brain].

Molecular forms of cathepsin D bound with subcellular structures were studied in the grey matter of the large hemispheres. Free and bound forms of the enzymes exposed to solubilization with detergent triton X-100 were fractionated by passage through a Sephadex G-100 column. Gel chromatographic analysis demonstrated three peaks of acid proteinase activity.