Target intelligence / Profile preview

Plasminogen receptor with a C-terminal lysine (PLGRKT)

Target
PLGRKT
Molecular classification
Receptor, Transmembrane protein, Other (functionally a co-receptor or platform for plasminogen activation on the cell surface)
01

Overview

Plasminogen receptor with a C-terminal lysine (PLGRKT) is an integral transmembrane protein that exposes a lysine at its C-terminus, enabling cell-surface binding and activation of plasminogen by plasminogen activators such as urokinase and tissue-type plasminogen activator. It is highly expressed on monocytes, macrophages, and some lymphocytes, and is upregulated during cell differentiation and inflammatory responses. PLGRKT plays a key role in regulating macrophage migration and recruitment, promotes matrix metalloproteinase activation, and participates in wound healing, tissue remodeling, cancer invasion/proliferation, and possibly metabolic regulation. While no drugs currently target PLGRKT directly, its cell-surface localization and critical role in plasminogen activation make it a promising therapeutic target, especially in inflammation and cancer.

Other names
Plg-RKTPlg-R(KT)PLG-RKTPlasminogen receptor (KT)C9orf46MDS030AD025FLJ146885033414D02RikUncharacterized hematopoietic stem/progenitor cells protein MDS030Transmembrane protein C9orf46Plasminogen receptor, C-terminal lysine transmembrane protein
02

Mechanism of action

Drugs or antibodies blocking PLGRKT prevent plasminogen binding and activation at the cell surface, thereby inhibiting downstream plasmin-dependent processes like cell migration, invasion, and cytokine release. Antagonists may reduce inflammation or metastasis by limiting macrophage recruitment and/or matrix degradation. Inhibitors of plasminogen activation (e.g., EACA) act by blocking lysine-binding sites (which include the C-terminal lysine on PLGRKT).

03

Biological functions

Plasminogen activationCell migrationRegulation of inflammatory responseMonocyte/macrophage recruitmentProhormone processingMatrix metalloprotease activation (MMP2, MMP9)Wound healingDevelopmentApoptosisCell proliferation
04

Disease associations

Cancer (regulation of invasion, metastasis, and apoptosis/proliferation)Inflammation (macrophage recruitment, wound healing)Metabolic homeostasis (adipose tissue function)Plasminogen deficiency type IOther (potential roles in infection, cardiovascular disease, tissue remodeling)
05

Safety considerations

Potential concern: Targeting PLGRKT or the plasminogen activation pathway could disrupt physiological wound healing, normal immune cell recruitment, and tissue remodeling, raising risks for impaired repair or immune responseModulation of plasminogen activation could affect risk of bleeding or thrombosis depending on context
06

Interacting drugs

None specifically approved or characterized as direct PLGRKT antagonists/agonists to date. Small-molecule inhibitors such as aminocaproic acid (EACA), amiloride, and aprotinin have been shown to inhibit functions linked to plasminogen activation and may indirectly modulate PLGRKT effects in cellular models

2 more in the full profile.

07

Biomarkers

Proinflammatory monocytes/macrophages in inflammation and wound healingSome cancers (e.g., breast cancer tissue)Plasminogen activation status on immune cells

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