Separation of Cerebroproteins of Human Brain

Bogoch, Samuel; Rajam, P. C.; Belval, Peter C.

doi:10.1038/204073b0

Cited by 32 publications

(4 citation statements)

References 7 publications

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“…7a). A striking result was that mice appear to lack 17 (29%) of the 58 molecularly-defined human lung cell populations, including many of the newly identified human molecular types (proximal ciliated (3); proximal (5), differentiating (6), and proliferating (7) basal; AT2-s (15); Cap-i1 (20) and i2 (21) capillary cells; bronchial vessel 1 (22) and 2 (23); fibromyocytes (28), lipofibroblasts (31); IGSF21+ (52), EREG+ (53), TREM2+ (54) dendritic cells; and OLR1+ monocytes (56)). Some of the missing cell populations might be rare (e.g.…”

Section: Loss Gain and Diversification Of Lung Cell Types And Gene Ementioning

confidence: 99%

“…Over the past two centuries, hundreds of human cell types have been discovered, categorized, and studied by microscopy, creating the classical atlases that provide the cellular foundation for modern medicine [1][2][3][4][5] . In the past several decades, cell-type-specific marker genes have been identified that supplement the histological descriptions and provide molecular definitions and functions of the cell types [6][7][8][9] . This reached its apex in the systematic profiling studies that elucidate genome-wide expression profiles of purified cell populations and, more recently, of individual cells by single cell RNA sequencing (scRNAseq) [10][11][12][13][14] .…”

Section: Introductionmentioning

confidence: 99%

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A molecular cell atlas of the human lung from single cell RNA sequencing

Travaglini

Nabhan

Penland

et al. 2019

Preprint

140

182

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Although single cell RNA sequencing studies have begun providing compendia of cell expression profiles, it has proven more difficult to systematically identify and localize all molecular cell types in individual organs to create a full molecular cell atlas. Here we describe droplet-and plate-based single cell RNA sequencing applied to ~70,000 human lung and blood cells, combined with a multi-pronged cell annotation approach, which have allowed us to define the gene expression profiles and anatomical locations of 58 cell populations in the human lung, including 41 of 45 previously known cell types or subtypes and 14 new ones. This comprehensive molecular atlas elucidates the biochemical functions of lung cell types and the cell-selective transcription factors and optimal markers for making and monitoring them; defines the cell targets of circulating hormones and predicts local signaling interactions including sources and targets of chemokines in immune cell trafficking and expression changes on lung homing; and identifies the cell types directly affected by lung disease genes. Comparison to mouse identified 17 molecular types that appear to have been gained or lost during lung evolution and others whose expression profiles have been substantially altered, revealing extensive plasticity of cell types and cell-type-specific gene expression during organ evolution including expression switches between cell types. This lung atlas provides the molecular foundation for investigating how lung cell identities, functions, and interactions are achieved in development and tissue engineering and altered in disease and evolution. certified by peer review)

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Section: Loss Gain and Diversification Of Lung Cell Types And Gene Ementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A molecular cell atlas of the human lung from single cell RNA sequencing

Travaglini

Nabhan

Penland

et al. 2019

Preprint

140

182

View full text Add to dashboard Cite

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“…Tissues. Most kinds of tissue have been analyzed electrophoretically: brain for proteins (253,646,1414,1543,1610,1700,1750,2020,2280, 2341, 2460), lipoproteins (744), a metal-bound lipoprotein (854) Electrophoresis is useful for studying the curing of pork (1727) and for identifying kinds of meats (1730). Lower Vertebrates.…”

Section: Glycoproteinsmentioning

confidence: 99%

Electrophoresis

Strickland¹

1966

Anal. Chem.

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“…Several workers have only recently turned their attention to developing preparative procedures that would serve to accomplish this purpose. Bogoch, Rajam & Belval (1964) have reported the separation of large quantities of protein from human grey matter by using DEAE-cellulose chromatography. Bondy & Perry (1963) used DEAE-cellulose to fractionate brain proteins in order to study the incorporation of isotope into individual fractions.…”

mentioning

confidence: 99%

Fractionation of brain macromolecules. Chromatography on hydroxyapatite of soluble proteins and nucleic acids from whole rat brain and the effect of autolysis

Brunngraber¹,

Occomy²

1965

Biochemical Journal

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1. A procedure for the chromatographic fractionation of soluble brain proteins on calcium hydroxyapatite is described. Chromatograms obtained are reproducible; approximately 11 protein and at least three nucleic acid components can be identified. The effects of column dimensions and flow rate on the chromatograms obtained are described. 2. One of the nucleic acid components appears to correspond to soluble RNA and another to ribosomal RNA. Treatment of homogenates by procedures that cause the removal of ribosomes from soluble extracts also cause the disappearance of the component corresponding to ribosomal RNA. Centrifugation of rat-brain homogenates prepared in 0.25m-sucrose at 105400g for 90min. causes the sedimentation of ribosomes as well as the disappearance of the component corresponding to ribosomal RNA. Extraction of brain tissue, or particulate fractions prepared from brain, with dilute buffers causes the solubilization of part of the ribosomal RNA that then can subsequently be identified in the chromatogram. 3. Autolysis under aerobic conditions has been shown to cause an increase in the nucleic acid component in the chromatogram that corresponds to the ribosomal RNA. Aerobic autolysis causes part of the ribosomal RNA to be solubilized, as evidenced by its failure to be sedimented by centrifugation at 105400g for 90min. and by its appearance in the fraction corresponding to ribosomal RNA in the chromatogram. These changes were not observed when autolysis was carried out under anaerobic conditions. Aerobic autolysis also caused changes in those proteins that are strongly adsorbed on the gel. 4. In general, the proteins of the cell sap appeared to be fairly stable to autolysis. Marked differences in the chromatograms are observed when soluble proteins from the particle fraction were autolysed and chromatographed.

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Separation of Cerebroproteins of Human Brain

Cited by 32 publications

References 7 publications

A molecular cell atlas of the human lung from single cell RNA sequencing

A molecular cell atlas of the human lung from single cell RNA sequencing

Electrophoresis

Fractionation of brain macromolecules. Chromatography on hydroxyapatite of soluble proteins and nucleic acids from whole rat brain and the effect of autolysis

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