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Article ; Online: Plasminogen activator receptor assemblies in cell signaling, innate immunity, and inflammation.

Gonias, Steven L

American journal of physiology. Cell physiology

2021 Volume 321, Issue 4, Page(s) C721–C734

Abstract: Tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA) are serine proteases and major activators of fibrinolysis in mammalian systems. Because fibrinolysis is an essential component of the response to tissue injury, ... ...

Abstract	Tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA) are serine proteases and major activators of fibrinolysis in mammalian systems. Because fibrinolysis is an essential component of the response to tissue injury, diverse cells, including cells that participate in the response to injury, have evolved receptor systems to detect tPA and uPA and initiate appropriate cell-signaling responses. Formation of functional receptor systems for the plasminogen activators requires assembly of diverse plasma membrane proteins, including but not limited to: the urokinase receptor (uPAR); integrins;
MeSH term(s)	Animals ; Enzyme Activation ; Fibrinolysis ; Humans ; Immunity, Innate ; Inflammation/immunology ; Inflammation/metabolism ; Inflammation Mediators/metabolism ; Ligands ; Plasminogen/metabolism ; Protein Conformation ; Receptors, Urokinase Plasminogen Activator/chemistry ; Receptors, Urokinase Plasminogen Activator/metabolism ; Signal Transduction ; Structure-Activity Relationship ; Tissue Plasminogen Activator/chemistry ; Tissue Plasminogen Activator/metabolism
Chemical Substances	Inflammation Mediators ; Ligands ; PLAUR protein, human ; Receptors, Urokinase Plasminogen Activator ; Plasminogen (9001-91-6) ; Tissue Plasminogen Activator (EC 3.4.21.68)
Language	English
Publishing date	2021-08-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00269.2021
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Article: Establishing priorities for implementation of large language models in pathology and laboratory medicine.

Arvisais-Anhalt, Simone / Gonias, Steven L / Murray, Sara G

Academic pathology

2024 Volume 11, Issue 1, Page(s) 100101

Abstract: Artificial intelligence and machine learning have numerous applications in pathology and laboratory medicine. The release of ChatGPT prompted speculation regarding the potentially transformative role of large-language models (LLMs) in academic pathology, ...

Abstract	Artificial intelligence and machine learning have numerous applications in pathology and laboratory medicine. The release of ChatGPT prompted speculation regarding the potentially transformative role of large-language models (LLMs) in academic pathology, laboratory medicine, and pathology education. Because of the potential to improve LLMs over the upcoming years, pathology and laboratory medicine clinicians are encouraged to embrace this technology, identify pathways by which LLMs may support our missions in education, clinical practice, and research, participate in the refinement of AI modalities, and design user-friendly interfaces that integrate these tools into our most important workflows. Challenges regarding the use of LLMs, which have already received considerable attention in a general sense, are also reviewed herein within the context of the pathology field and are important to consider as LLM applications are identified and operationalized.
Language	English
Publishing date	2024-01-11
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2819382-9
ISSN	2374-2895
ISSN	2374-2895
DOI	10.1016/j.acpath.2023.100101
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Article: Schwann cell extracellular vesicles: judging a book by its cover.

Gonias, Steven L / Campana, Wendy M

Neural regeneration research

2022 Volume 18, Issue 2, Page(s) 325–326

Language	English
Publishing date	2022-08-24
Publishing country	India
Document type	Journal Article
ZDB-ID	2388460-5
ISSN	1876-7958 ; 1673-5374
ISSN (online)	1876-7958
ISSN	1673-5374
DOI	10.4103/1673-5374.346478
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Article ; Online: Hepatocyte tPA: where have you been hiding?

Gonias, Steven L

Blood

2019 Volume 133, Issue 7, Page(s) 631–632

MeSH term(s)	Fibrinolysis ; Hepatocytes
Language	English
Publishing date	2019-02-14
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood-2018-12-891515
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Article ; Online: Mechanisms by Which LRP1 (Low-Density Lipoprotein Receptor-Related Protein-1) Maintains Arterial Integrity.

Gonias, Steven L

Arteriosclerosis, thrombosis, and vascular biology

2018 Volume 38, Issue 11, Page(s) 2548–2549

MeSH term(s)	Calcium ; Cytoskeletal Proteins ; Cytoskeleton ; Lipoproteins, LDL ; Low Density Lipoprotein Receptor-Related Protein-1
Chemical Substances	Cytoskeletal Proteins ; Lipoproteins, LDL ; Low Density Lipoprotein Receptor-Related Protein-1 ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2018-08-02
Publishing country	United States
Document type	Editorial ; Research Support, N.I.H., Extramural ; Comment
ZDB-ID	1221433-4
ISSN	1524-4636 ; 1079-5642
ISSN (online)	1524-4636
ISSN	1079-5642
DOI	10.1161/ATVBAHA.118.311882
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Zs.A 1705: Show issues

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Article ; Online: An LRP1-binding motif in cellular prion protein replicates cell-signaling activities of the full-length protein.

Mantuano, Elisabetta / Zampieri, Carlotta / Azmoon, Pardis / Gunner, Cory B / Heye, Kyle R / Gonias, Steven L

JCI insight

2023 Volume 8, Issue 15

Abstract: Low-density lipoprotein receptor-related protein-1 (LRP1) functions as a receptor for nonpathogenic cellular prion protein (PrPC), which is released from cells by ADAM (a disintegrin and metalloproteinase domain) proteases or in extracellular vesicles. ... ...

Abstract	Low-density lipoprotein receptor-related protein-1 (LRP1) functions as a receptor for nonpathogenic cellular prion protein (PrPC), which is released from cells by ADAM (a disintegrin and metalloproteinase domain) proteases or in extracellular vesicles. This interaction activates cell signaling and attenuates inflammatory responses. We screened 14-mer PrPC-derived peptides and identified a putative LRP1 recognition motif in the PrPC sequence spanning residues 98-111. A synthetic peptide (P3) corresponding to this region replicated the cell-signaling and biological activities of full-length shed PrPC. P3 blocked LPS-elicited cytokine expression in macrophages and microglia and rescued the heightened sensitivity to LPS in mice in which the PrPC gene (Prnp) had been deleted. P3 activated ERK1/2 and induced neurite outgrowth in PC12 cells. The response to P3 required LRP1 and the NMDA receptor and was blocked by the PrPC-specific antibody, POM2. P3 has Lys residues, which are typically necessary for LRP1 binding. Converting Lys100 and Lys103 into Ala eliminated the activity of P3, suggesting that these residues are essential in the LRP1-binding motif. A P3 derivative in which Lys105 and Lys109 were converted into Ala retained activity. We conclude that the biological activities of shed PrPC, attributed to interaction with LRP1, are retained in synthetic peptides, which may be templates for therapeutics development.
MeSH term(s)	Rats ; Mice ; Animals ; Prion Proteins ; Receptors, Lipoprotein ; Lipopolysaccharides ; Signal Transduction ; Prions/metabolism ; PC12 Cells
Chemical Substances	Prion Proteins ; Receptors, Lipoprotein ; Lipopolysaccharides ; Prions
Language	English
Publishing date	2023-08-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.170121
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Article ; Online: Plasminogen Receptors in Human Malignancies: Effects on Prognosis and Feasibility as Targets for Drug Development.

Gonias, Steven L / Zampieri, Carlotta

Current drug targets

2019 Volume 21, Issue 7, Page(s) 647–656

Abstract: The major proteases that constitute the fibrinolysis system are tightly regulated. Protease inhibitors target plasmin, the protease responsible for fibrin degradation, and the proteases that convert plasminogen into plasmin, including tissue-type ... ...

Abstract	The major proteases that constitute the fibrinolysis system are tightly regulated. Protease inhibitors target plasmin, the protease responsible for fibrin degradation, and the proteases that convert plasminogen into plasmin, including tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA). A second mechanism by which fibrinolysis is regulated involves exosite interactions, which localize plasminogen and its activators to fibrin, extracellular matrix (ECM) proteins, and cell surfaces. Once plasmin is generated in association with cell surfaces, it may cleave transmembrane proteins, activate growth factors, release growth factors from ECM proteins, remodel ECM, activate metalloproteases, and trigger cell-signaling by cleaving receptors in the Proteaseactivated Receptor (PAR) family. These processes are all implicated in cancer. It is thus not surprising that a family of structurally diverse but functionally similar cell-surface proteins, called Plasminogen Receptors (PlgRs), which increase the catalytic efficiency of plasminogen activation, have received attention for their possible function in cancer and as targets for anticancer drug development. In this review, we consider four previously described PlgRs, including: α-enolase, annexin-A2, Plg-RKT, and cytokeratin-8, in human cancer. To compare the PlgRs, we mined transcriptome profiling data from The Cancer Genome Atlas (TCGA) and searched for correlations between PlgR expression and patient survival. In glioma, the expression of specific PlgRs correlates with tumor grade. In a number of malignancies, including glioblastoma and liver cancer, increased expression of α-enolase or annexin-A2 is associated with an unfavorable prognosis. Whether these correlations reflect the function of PlgRs as receptors for plasminogen or other activities is discussed.
MeSH term(s)	Animals ; Fibrinolysis/physiology ; Humans ; Molecular Targeted Therapy ; Neoplasm Grading ; Neoplasms/genetics ; Neoplasms/metabolism ; Neoplasms/therapy ; Prognosis ; Receptors, Proteinase-Activated/biosynthesis ; Receptors, Proteinase-Activated/genetics ; Receptors, Urokinase Plasminogen Activator/biosynthesis ; Receptors, Urokinase Plasminogen Activator/genetics
Chemical Substances	Receptors, Proteinase-Activated ; Receptors, Urokinase Plasminogen Activator
Language	English
Publishing date	2019-11-21
Publishing country	United Arab Emirates
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2064859-5
ISSN	1873-5592 ; 1389-4501
ISSN (online)	1873-5592
ISSN	1389-4501
DOI	10.2174/1389450120666191122101658
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Zs.A 5578: Show issues

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Article ; Online: The LRP1/CD91 ligands, tissue-type plasminogen activator, α

Mantuano, Elisabetta / Azmoon, Pardis / Banki, Michael A / Gunner, Cory B / Gonias, Steven L

Scientific reports

2022 Volume 12, Issue 1, Page(s) 17594

Abstract: LDL Receptor-related Protein-1 (LRP1/CD91) binds diverse ligands, many of which activate cell-signaling. Herein, we compared three LRP1 ligands that inhibit inflammatory responses triggered by lipopolysaccharide (LPS), including: enzymatically-inactive ... ...

Abstract	LDL Receptor-related Protein-1 (LRP1/CD91) binds diverse ligands, many of which activate cell-signaling. Herein, we compared three LRP1 ligands that inhibit inflammatory responses triggered by lipopolysaccharide (LPS), including: enzymatically-inactive tissue-type plasminogen activator (EI-tPA); activated α
MeSH term(s)	Pregnancy ; Female ; Humans ; Lipopolysaccharides ; Ligands ; Prion Proteins/metabolism ; Tissue Plasminogen Activator/metabolism ; Pregnancy-Associated alpha 2-Macroglobulins/metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Low Density Lipoprotein Receptor-Related Protein-1/metabolism ; Cytokines/metabolism
Chemical Substances	Lipopolysaccharides ; Ligands ; Prion Proteins ; Tissue Plasminogen Activator (EC 3.4.21.68) ; Pregnancy-Associated alpha 2-Macroglobulins ; Receptors, N-Methyl-D-Aspartate ; Low Density Lipoprotein Receptor-Related Protein-1 ; Cytokines ; LRP1 protein, human
Language	English
Publishing date	2022-10-20
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-22498-1
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Article ; Online: An antibody that targets cell-surface glucose-regulated protein-78 inhibits expression of inflammatory cytokines and plasminogen activator inhibitors by macrophages.

Gunner, Cory B / Azmoon, Pardis / Mantuano, Elisabetta / Das, Lipsa / Zampieri, Carlotta / Pizzo, Salvatore V / Gonias, Steven L

Journal of cellular biochemistry

2023 Volume 124, Issue 5, Page(s) 743–752

Abstract: Glucose-regulated protein-78 (Grp78) is an endoplasmic reticulum chaperone, which is secreted by cells and associates with cell surfaces, where it functions as a receptor for activated ... ...

Abstract	Glucose-regulated protein-78 (Grp78) is an endoplasmic reticulum chaperone, which is secreted by cells and associates with cell surfaces, where it functions as a receptor for activated α
MeSH term(s)	Humans ; Cytokines/metabolism ; Membrane Proteins/metabolism ; Plasminogen Inactivators/metabolism ; Diabetes Mellitus, Type 2/metabolism ; Endoplasmic Reticulum Chaperone BiP ; N-Methylaspartate/metabolism ; Macrophages/metabolism ; Antibodies ; Low Density Lipoprotein Receptor-Related Protein-1/genetics ; Low Density Lipoprotein Receptor-Related Protein-1/metabolism
Chemical Substances	Cytokines ; Membrane Proteins ; Plasminogen Inactivators ; Endoplasmic Reticulum Chaperone BiP ; N-Methylaspartate (6384-92-5) ; Antibodies ; Low Density Lipoprotein Receptor-Related Protein-1
Language	English
Publishing date	2023-03-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	392402-6
ISSN	1097-4644 ; 0730-2312
ISSN (online)	1097-4644
ISSN	0730-2312
DOI	10.1002/jcb.30401
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Zs.A 1114: Show issues

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Article ; Online: Axon-derived PACSIN1 binds to the Schwann cell survival receptor, LRP1, and transactivates TrkC to promote gliatrophic activities.

Martellucci, Stefano / Flütsch, Andreas / Carter, Mark / Norimoto, Masaki / Pizzo, Donald / Mantuano, Elisabetta / Sadri, Mahrou / Wang, Zixuan / Chillin-Fuentes, Daisy / Rosenthal, Sara Brin / Azmoon, Pardis / Gonias, Steven L / Campana, Wendy M

Glia

2024 Volume 72, Issue 5, Page(s) 916–937

Abstract: Schwann cells (SCs) undergo phenotypic transformation and then orchestrate nerve repair following PNS injury. The ligands and receptors that activate and sustain SC transformation remain incompletely understood. Proteins released by injured axons ... ...

Abstract	Schwann cells (SCs) undergo phenotypic transformation and then orchestrate nerve repair following PNS injury. The ligands and receptors that activate and sustain SC transformation remain incompletely understood. Proteins released by injured axons represent important candidates for activating the SC Repair Program. The low-density lipoprotein receptor-related protein-1 (LRP1) is acutely up-regulated in SCs in response to injury, activating c-Jun, and promoting SC survival. To identify novel LRP1 ligands released in PNS injury, we applied a discovery-based approach in which extracellular proteins in the injured nerve were captured using Fc-fusion proteins containing the ligand-binding motifs of LRP1 (CCR2 and CCR4). An intracellular neuron-specific protein, Protein Kinase C and Casein Kinase Substrate in Neurons (PACSIN1) was identified and validated as an LRP1 ligand. Recombinant PACSIN1 activated c-Jun and ERK1/2 in cultured SCs. Silencing Lrp1 or inhibiting the LRP1 cell-signaling co-receptor, the NMDA-R, blocked the effects of PACSIN1 on c-Jun and ERK1/2 phosphorylation. Intraneural injection of PACSIN1 into crush-injured sciatic nerves activated c-Jun in wild-type mice, but not in mice in which Lrp1 is conditionally deleted in SCs. Transcriptome profiling of SCs revealed that PACSIN1 mediates gene expression events consistent with transformation to the repair phenotype. PACSIN1 promoted SC migration and viability following the TNFα challenge. When Src family kinases were pharmacologically inhibited or the receptor tyrosine kinase, TrkC, was genetically silenced or pharmacologically inhibited, PACSIN1 failed to induce cell signaling and prevent SC death. Collectively, these studies demonstrate that PACSIN1 is a novel axon-derived LRP1 ligand that activates SC repair signaling by transactivating TrkC.
MeSH term(s)	Animals ; Mice ; Rats ; Axons ; Cell Survival ; Cells, Cultured ; Ligands ; Rats, Sprague-Dawley ; Receptor Protein-Tyrosine Kinases/metabolism ; Schwann Cells/metabolism ; Humans ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Adaptor Proteins, Signal Transducing/pharmacology ; Recombinant Proteins
Chemical Substances	Ligands ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; PACSIN1 protein, human ; Adaptor Proteins, Signal Transducing ; Recombinant Proteins
Language	English
Publishing date	2024-02-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	639414-0
ISSN	1098-1136 ; 0894-1491
ISSN (online)	1098-1136
ISSN	0894-1491
DOI	10.1002/glia.24510
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