[16][18] Though ARPP and CARP proteins show significant homology, their expression profiles in muscle cells are markedly different; CARP is expressed throughout atria and ventricles, in development and in adult myocytes, however ARPP is almost exclusively ventricular and only in adult myocytes.

In mice lacking all three muscle ankyrin repeat proteins (MARPs), ARPP, CARP, and DARP), skeletal muscles tended towards a more slower fiber type distribution, with longer resting sarcomere length, decreased fiber stiffness, expression of a longer titin isoform, greater degree of torque loss following eccentric contraction-related injury, and enhanced expression of MyoD and MLP.

[24] In a mouse model of muscular dystrophy with myositis (mdm) caused by a small deletion in titin, ANKRD2 mRNA expression was shown to be significantly elevated in skeletal muscle tissue along with that of CARP, suggesting a role for ARPP in titin-based signaling.

[28] ARPP has also been shown to be a potentially useful biomarker for the differential diagnosis between oncocytoma and chromophobe renal cell carcinomas.

[29] In non-pathologic physiology, ARPP mRNA expression in skeletal muscle of patients was shown to be elevated two days following fatiguing jumping exercises.

[30] Ankrd2 has been shown to be involved in the progression of some types of cancers, such as osteosarcoma[9] and head and neck squamous cell carcinoma.