Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation and metal homeostasis.

Copper (Cu) is essential for respiration, neurotransmitter synthesis, oxidative stress response, and transcription regulation, with imbalances leading to neurological, cognitive, and muscular disorders. Here we show the role of a novel Cu-binding protein (Cu-BP) in mammalian transcriptional regulation, specifically on skeletal muscle differentiation using murine primary myoblasts. Utilizing synchrotron X-ray fluorescence-mass spectrometry, we identified murine cysteine-rich intestinal protein 2 (mCrip2) as a key Cu-BP abundant in both nuclear and cytosolic fractions.

Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation.

Copper (Cu) is an essential trace element required for respiration, neurotransmitter synthesis, oxidative stress response, and transcriptional regulation. Imbalance in Cu homeostasis can lead to several pathological conditions, affecting neuronal, cognitive, and muscular development. Mechanistically, Cu and Cu-binding proteins (Cu-BPs) have an important but underappreciated role in transcription regulation in mammalian cells.

Study of pH and Thermodynamic Parameters via Circular Dichroism Spectroscopy of a Recombinant Human Lactoferrin.

The production of human recombinant proteins to be used for therapeutic or nutritional purposes must focus on obtaining a molecule that is as close as possible to the native human protein. This biotechnological tool has been documented in various studies published in recent decades, with lactoferrin being one of those that has generated the most interest, being a promising option for recombinant technology. However, stability studies including thermodynamic parameters have not been reported for recombinant lactoferrin (Lf).

Biological activity of mixed chelate copper(II) complexes, with substituted diimine and tridentate Schiff bases (NNO) and their hydrogenated derivatives as secondary ligands: Casiopeína's fourth generation.

We synthesize and characterize nine copper(II) compounds. Four with general formula [Cu(NNO)(NO)] and five mixed chelates [Cu(NNO)(N-N)], where NNO corresponds to asymmetric salen ligands (E)-2-((2-(methylamino)ethylimino)methyl)phenolate (L1) and (E)-3-((2-(methylamino)ethylimino)methyl)naphthalenolate (LN1); and their hydrogenated derivatives 2-((2-(methylamino)ethylamino)methyl)phenolate (LH1) and 3-((2-(methylamino)ethylamino)methyl)naphthalenolate (LNH1); and N-N correspond to 4,4'-dimethyl-2,2'-bipiridyne(dmbpy) or 1,10-phenanthroline (phen). Using EPR, the geometries of the compounds in solution in DMSO were assigned, [Cu(LN1)(NO)] and [Cu(LNH1)(NO)] a square-planar, [Cu(L1)(NO)], [Cu(LH1)(NO)], [Cu(L1)(dmby)] and [Cu(LH1)(dmby)] a square-based pyramid; and [Cu(LN1)(dmby)], [Cu(LNH1)(dmby)] and [Cu(L1)(phen)] and elongated octahedral.

Electrochemical and CD-spectroelectrochemical studies of the interaction between BSA and the complex [Cu(Bztpen)], (Bztpen = (N-benzyl-N, N', N'-tris (pyridin-2-ylmethyl) ethylenediamine).

In this work we report the electrochemical, spectroscopical and spectro-electrochemical studies of a model complex [Cu(Bztpen)], (Bztpen = (N-benzyl-N,N',N'-tris(pyridin-2-ylmethyl)ethylenediamine) in order to propose a methodology to evaluate the interaction of potential metal based anticancer agents during electron transfer processes, with transport proteins such as Bovine Serum Albumin (BSA). It was possible to establish a reversible electron transfer [Cu(Bztpen)] +1e → [Cu(Bztpen)] and a weak interaction energy between BSA and [Cu(Bztpen)] and [Cu(Bztpen)] species, with no adsorption of protein over the electrode surface. Circular Dichroism (CD) Spectroelectrochemistry, not reported before, reveals no significant changes in BSA structure during the electron transfer [Cu(Bztpen)] + 1e → [Cu(Bztpen)].